Xiaohe Tong - Academia.edu (original) (raw)
Papers by Xiaohe Tong
Peptides: The Wave of the Future, 2001
A farnesylated 9-aa peptide, H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH, comes from the C... more A farnesylated 9-aa peptide, H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH, comes from the C-terminus of K-Ras, which is the most frequently mutated member in human tumours. The hRCE1 protease cleaved H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH between the Cys(farnesyl) and Val positons, generating H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-OH and H-Val-Ile-Met-OH as products. For developing a useful direct fluorogenic assay for both cloned hRCEl analysis and inhibitor discovery, we synthesized twenty K-Ras-derived peptides for screening [1]. Some peptides (Table 1) were modified with either (7-Methyloxy-coumarin-4-yl)acetyl (Mca) or 2-Aminobenzoyl (Abz) fluorescent chromophores at the N-terminus, and quenching-group-containing amino acids at the amino acid position of H-Val-Ile-Met-OH. The quenching-group-containing amino acids used were either N β-2,4-dinitrophenyl-L-di-aminopropionic acid [Dap(Dnp)] or Ne-2,4-dinitrophenyl-L-lysine [Lys(Dnp)].
Journal of Biological Chemistry, 2000
To characterize the sites in human p53 that become phosphorylated in response to DNA damage, we h... more To characterize the sites in human p53 that become phosphorylated in response to DNA damage, we have developed polyclonal antibodies that recognize p53 only when it is phosphorylated at specific sites. Several attempts to generate an antibody to p53 phosphorylated at Ser 6 using a phosphoserine-containing peptide as an immunogen were unsuccessful; however, phosphorylation-specific antibodies were produced by using the phosphoserine mimetic, L-2-amino-4-phosphono-4,4-difluorobutanoic acid (F 2 Pab), in place of phosphoserine. Fmoc-F 2 Pab was prepared by an improved synthesis and chemically incorporated using solid phase peptide synthesis. Affinity-purified antibodies elicited by immunizing rabbits with an F 2 Pab peptide coupled to keyhole limpet hemocyanin recognized a p53(1-39) peptide phosphorylated only at Ser 6 but not the unphosphorylated peptide or the same peptide phosphorylated at Ser 9 , Ser 15 , Ser 20 , Ser 33 , or Ser 37. Untreated A549 cells exhibited a background of constitutive phosphorylation at Ser 6 that increased approximately 10-fold upon exposure to either ionizing radiation or UV light. Similar results were obtained for Ser 9 using antibodies raised against a conventional phosphopeptide. Ser 9 was phosphorylated by casein kinase 1 in vitro in a phosphoserine 6-dependent manner. Our data identify two additional DNA damage-induced phosphorylations in human p53 and show that F 2 Pab-derivatized peptides can be used to develop phosphorylation site-specific polyclonal antibodies.
Understanding Biology Using Peptides
... Xiaohe Tong, Ling Sheng, Xiaofen Zhong, Yi Tang, Junge Lu, Zhenjun Diwu and Anita Hong ... Al... more ... Xiaohe Tong, Ling Sheng, Xiaofen Zhong, Yi Tang, Junge Lu, Zhenjun Diwu and Anita Hong ... Although a fluorescence resonance energy transfer (FRET) depsipeptide, Ac-DED(Edans)EE-αAbuψ[COO]ASK(Dabcyl)-NH2 (substrate I) is widely used for detecting HCV NS3/4A ...
Tetrahedron Letters, 2000
Abstract An efficient method for the solid phase synthesis of aspartyl aldehyde peptides has been... more Abstract An efficient method for the solid phase synthesis of aspartyl aldehyde peptides has been developed. It uses a low cost synthetic process for the preparation of Fmoc-protected Weinreb amide linker. This procedure covers several tetrapeptide aspartyl aldehydes as well as biotinylated tetrapeptide aspartyl aldehydes.
Proceedings of the Japan Academy, Series B, 2011
There is a significant need for antibodies that can bind targets with greater affinity. Here we d... more There is a significant need for antibodies that can bind targets with greater affinity. Here we describe a novel strategy employing chemical semisynthesis to produce symmetroadhesins: antibody-like molecules having nonprotein hinge regions that are more flexible and extendible and are capable of two-handed binding. Native chemical ligation was carried out under mild, non-denaturing conditions to join a ligand binding domain (AO peptide) to an IgG1 Fc dimer via discrete oxyethylene oligomers of various lengths. Two-handed AO-Fc fusion proteins were obtained in quantitative yield and shown by surface plasmon resonance to bind an anti-AO antibody with a K D at least two orders of magnitude greater than the cognate AO peptide. MALDI-TOF MS analysis confirmed the protein/nonprotein/protein structure of the two-handed molecules, demonstrating its power to characterize complex protein-nonprotein hybrids by virtue of desorption/ionization mediated by peptide sequences contained therein. We anticipate many applications for symmetroadhesins that combine the target specificity of antibodies with the novel physical, chemical and biological properties of nonprotein hinges.
Journal of Neuropathology and Experimental Neurology, 2007
The Alzheimer disease (AD) brain pathology is characterized by extracellular deposits of amyloid-... more The Alzheimer disease (AD) brain pathology is characterized by extracellular deposits of amyloid-A (AA) peptides and intraneuronal fibrillar structures. These pathological features may be functionally linked, but the mechanism by which AA accumulation relates to neuronal degeneration is still poorly understood. AA peptides are fragments cleaved from the amyloid precursor protein (APP), a type I transmembrane protein ubiquitously expressed in the nervous system. Although the proteolytic processing of APP has been implicated in the pathogenesis of AD, the normal function of APP, whether this function is related to the proteolytic processing, and where this processing takes place in neurons remain unknown. APP is anterogradely transported along the axon apparently on cytoskeletal tracks. Moreover, several studies indicate that APP processing may occur within axonal or presinaptic terminals, supporting the hypothesis that APP functions as a vesicular receptor for cytoskeletal motor proteins. In the current study, we test the hypothesis that myosin II, important contributor to the cytoskeleton of neuronal cells, may influence the trafficking and/or the processing of APP. Our results demonstrate that down-regulation of myosin II-B, the major myosin isoform in neurons, is able to increase AA secretion, concomitantly altering the subcellular localization of APP. These new insights might be important for the understanding of the function of APP and provide a novel conceptual framework in which to analyze its pathological role. Work funded by grants from COFIN 2004 (no. 2004068928_003 and no. 2004063943_001).
American Journal of Veterinary Research, 2009
Objective-To evaluate the use of a commercially available 5-carboxyfluorescein-based, intramolecu... more Objective-To evaluate the use of a commercially available 5-carboxyfluorescein-based, intramolecularly quenched, fluorescence resonance energy transfer (FRET) peptide substrate of renin for measurement of plasma renin concentration in cats. Sample Population-Plasma samples obtained during a previous study of renal autograft ischemia-reperfusion injury in 10 cats and samples of fetal bovine serum containing recombinant human renin (rh-renin). Procedures-Experiments involving samples of fetal bovine serum containing rh-renin were conducted to identify a suitable control vehicle, optimal substrate concentration, and appropriate duration of incubation. With the use of the identified assay conditions, a standard curve was constructed to allow conversion of relative fluorescent units into values of renin concentration (ng/mL). Subsequently, plasma samples obtained from cats before and after renal autograft ischemia-reperfusion injury were assayed to determine endogenous renin concentration. Results-Under conditions of a 1:50 substrate dilution and 4-hour incubation period, the assay detected small amounts of rh-renin in fetal bovine serum. A linear relationship (R 2 = 0.996) between the relative fluorescent units generated and exogenous rh-renin concentration was evident. The assay detected renin in plasma samples obtained from cats after renal autograft ischemia-reperfusion, and renin concentrations on days 1 and 2 after transplant differed significantly. Conclusions and Clinical Relevance-The study data indicated that the assay involving the FRET peptide substrate of renin is potentially a rapid and specific method for measurement of plasma renin concentration in cats.
Retrovirology, Jan 15, 2013
Previously, we reported the conversion of the 12-mer linear and cell-impermeable peptide CAI to a... more Previously, we reported the conversion of the 12-mer linear and cell-impermeable peptide CAI to a cell-penetrating peptide NYAD-1 by using an i,i + 4 hydrocarbon stapling technique and confirmed its binding to the C-terminal domain (CTD) of the HIV-1 capsid (CA) protein with an improved affinity (K(d) ~ 1 μM) compared to CAI (K(d) ~ 15 μM). NYAD-1 disrupts the formation of both immature- and mature-like virus particles in in vitro and cell-based assembly assays. In addition, it displays potent anti-HIV-1 activity in cell culture against a range of laboratory-adapted and primary HIV-1 isolates. In this report, we expanded the study to i,i + 7 hydrocarbon-stapled peptides to delineate their mechanism of action and antiviral activity. We identified three potent inhibitors, NYAD-36, -66 and -67, which showed strong binding to CA in NMR and isothermal titration calorimetry (ITC) studies and disrupted the formation of mature-like particles. They showed typical α-helical structures and pen...
Journal of Molecular Biology, 2008
Advances in Experimental Medicine and Biology, 2009
SARS-CoV-2 uses human angiotensin-converting enzyme 2 (ACE2) as the primary receptor to enter hos... more SARS-CoV-2 uses human angiotensin-converting enzyme 2 (ACE2) as the primary receptor to enter host cells and initiate the infection. The critical binding region of ACE2 is a ∼30 aa long helix. Here we report the design of four stapled peptides based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection. All stapled peptides showed high helical contents (50-94% helicity). On the contrary, the linear control peptide NYBSP-C showed no helicity (19%). We have evaluated the peptides in a pseudovirus based single-cycle assay in HT1080/ACE2 and human lung cells A549/ACE2, overexpressing ACE2. Three of the four stapled peptides showed potent antiviral activity in HT1080/ACE2 (IC50: 1.9 – 4.1 µM) and A549/ACE2 cells (IC50: 2.2 – 2.8 µM). The linear peptides NYBSP-C and the double-stapled peptide StRIP16, used as controls, showed no antiviral activity. Most significantly, none of the stapled peptides show...
Med. Chem. Commun., 2016
Herein, we describe the design and synthesis of a novel BODIPY-labelled minihepcidin peptide to e... more Herein, we describe the design and synthesis of a novel BODIPY-labelled minihepcidin peptide to enable the high content analysis of ferroportin (SLC40A1) pharmacology.
The Faseb Journal, Mar 1, 2008
The Faseb Journal, Apr 1, 2009
Bioorganic & Medicinal Chemistry, 2015
One of the most critical requirements of the infection of the human immunodeficiency virus type 1... more One of the most critical requirements of the infection of the human immunodeficiency virus type 1 (HIV-1) is the interaction of its surface envelope glycoprotein gp120 with the cellular receptor CD4, which initiates virus entry to cells. Therefore, envelope glycoprotein gp120 has been validated as a potential target to develop HIV-1 entry inhibitors. Here we report the evaluation of a novel non-natural amino acid, termed 882376, reported earlier as a precursor of a CD4-mimetic miniprotein, as HIV-1 entry inhibitor. 882376 showed HIV-1 inhibitory activity against a large panel of primary isolates of different subtype. Moreover, genotyping of 882376 resistant HIV-1 virus revealed three amino acid substitutions in the gp120 including one in the CD4 binding site suggesting that this molecule may bind to gp120 and prevent its binding to CD4. Additional neutralization experiments indicate that 882376 is not active against mutant pseudoviruses carrying the amino acid substitutions S375H and S375Y located in the 'Phe43 cavity' which is the major site of CD4 binding, suggesting that this compound may interfere with the interaction between gp120 and CD4. The unnatural amino acid, 882376, is expected to serve as a lead for further optimization to more potent HIV-1 entry inhibitors.
Peptides: The Wave of the Future, 2001
Peptides Across the Pacific: The Proceedings of the Twenty-Third American and the Sixth International Peptide Symposium, 2013
We extend to you a warm and sunny Aloha in celebration of the 23 rd American Peptide Symposium an... more We extend to you a warm and sunny Aloha in celebration of the 23 rd American Peptide Symposium and the 6 th International Symposium. The meeting theme, Peptides Across the Pacific, embraced the spirit of the scientific and social program. Peptides Across the Pacific encompassed the important role that peptide science currently plays in so many disciplines and explored the potential impact peptides can make in scientific fields that have yet to realize the utility of these wonderful molecules. The scientific program for 2013 was framed by distinguished lectures delivered by two renowned peptide chemists.
Peptides: The Wave of the Future, 2001
A farnesylated 9-aa peptide, H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH, comes from the C... more A farnesylated 9-aa peptide, H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH, comes from the C-terminus of K-Ras, which is the most frequently mutated member in human tumours. The hRCE1 protease cleaved H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-Val-Ile-Met-OH between the Cys(farnesyl) and Val positons, generating H-Lys-Ser-Lys-Thr-Lys-Cys(farnesyl)-OH and H-Val-Ile-Met-OH as products. For developing a useful direct fluorogenic assay for both cloned hRCEl analysis and inhibitor discovery, we synthesized twenty K-Ras-derived peptides for screening [1]. Some peptides (Table 1) were modified with either (7-Methyloxy-coumarin-4-yl)acetyl (Mca) or 2-Aminobenzoyl (Abz) fluorescent chromophores at the N-terminus, and quenching-group-containing amino acids at the amino acid position of H-Val-Ile-Met-OH. The quenching-group-containing amino acids used were either N β-2,4-dinitrophenyl-L-di-aminopropionic acid [Dap(Dnp)] or Ne-2,4-dinitrophenyl-L-lysine [Lys(Dnp)].
Journal of Biological Chemistry, 2000
To characterize the sites in human p53 that become phosphorylated in response to DNA damage, we h... more To characterize the sites in human p53 that become phosphorylated in response to DNA damage, we have developed polyclonal antibodies that recognize p53 only when it is phosphorylated at specific sites. Several attempts to generate an antibody to p53 phosphorylated at Ser 6 using a phosphoserine-containing peptide as an immunogen were unsuccessful; however, phosphorylation-specific antibodies were produced by using the phosphoserine mimetic, L-2-amino-4-phosphono-4,4-difluorobutanoic acid (F 2 Pab), in place of phosphoserine. Fmoc-F 2 Pab was prepared by an improved synthesis and chemically incorporated using solid phase peptide synthesis. Affinity-purified antibodies elicited by immunizing rabbits with an F 2 Pab peptide coupled to keyhole limpet hemocyanin recognized a p53(1-39) peptide phosphorylated only at Ser 6 but not the unphosphorylated peptide or the same peptide phosphorylated at Ser 9 , Ser 15 , Ser 20 , Ser 33 , or Ser 37. Untreated A549 cells exhibited a background of constitutive phosphorylation at Ser 6 that increased approximately 10-fold upon exposure to either ionizing radiation or UV light. Similar results were obtained for Ser 9 using antibodies raised against a conventional phosphopeptide. Ser 9 was phosphorylated by casein kinase 1 in vitro in a phosphoserine 6-dependent manner. Our data identify two additional DNA damage-induced phosphorylations in human p53 and show that F 2 Pab-derivatized peptides can be used to develop phosphorylation site-specific polyclonal antibodies.
Understanding Biology Using Peptides
... Xiaohe Tong, Ling Sheng, Xiaofen Zhong, Yi Tang, Junge Lu, Zhenjun Diwu and Anita Hong ... Al... more ... Xiaohe Tong, Ling Sheng, Xiaofen Zhong, Yi Tang, Junge Lu, Zhenjun Diwu and Anita Hong ... Although a fluorescence resonance energy transfer (FRET) depsipeptide, Ac-DED(Edans)EE-αAbuψ[COO]ASK(Dabcyl)-NH2 (substrate I) is widely used for detecting HCV NS3/4A ...
Tetrahedron Letters, 2000
Abstract An efficient method for the solid phase synthesis of aspartyl aldehyde peptides has been... more Abstract An efficient method for the solid phase synthesis of aspartyl aldehyde peptides has been developed. It uses a low cost synthetic process for the preparation of Fmoc-protected Weinreb amide linker. This procedure covers several tetrapeptide aspartyl aldehydes as well as biotinylated tetrapeptide aspartyl aldehydes.
Proceedings of the Japan Academy, Series B, 2011
There is a significant need for antibodies that can bind targets with greater affinity. Here we d... more There is a significant need for antibodies that can bind targets with greater affinity. Here we describe a novel strategy employing chemical semisynthesis to produce symmetroadhesins: antibody-like molecules having nonprotein hinge regions that are more flexible and extendible and are capable of two-handed binding. Native chemical ligation was carried out under mild, non-denaturing conditions to join a ligand binding domain (AO peptide) to an IgG1 Fc dimer via discrete oxyethylene oligomers of various lengths. Two-handed AO-Fc fusion proteins were obtained in quantitative yield and shown by surface plasmon resonance to bind an anti-AO antibody with a K D at least two orders of magnitude greater than the cognate AO peptide. MALDI-TOF MS analysis confirmed the protein/nonprotein/protein structure of the two-handed molecules, demonstrating its power to characterize complex protein-nonprotein hybrids by virtue of desorption/ionization mediated by peptide sequences contained therein. We anticipate many applications for symmetroadhesins that combine the target specificity of antibodies with the novel physical, chemical and biological properties of nonprotein hinges.
Journal of Neuropathology and Experimental Neurology, 2007
The Alzheimer disease (AD) brain pathology is characterized by extracellular deposits of amyloid-... more The Alzheimer disease (AD) brain pathology is characterized by extracellular deposits of amyloid-A (AA) peptides and intraneuronal fibrillar structures. These pathological features may be functionally linked, but the mechanism by which AA accumulation relates to neuronal degeneration is still poorly understood. AA peptides are fragments cleaved from the amyloid precursor protein (APP), a type I transmembrane protein ubiquitously expressed in the nervous system. Although the proteolytic processing of APP has been implicated in the pathogenesis of AD, the normal function of APP, whether this function is related to the proteolytic processing, and where this processing takes place in neurons remain unknown. APP is anterogradely transported along the axon apparently on cytoskeletal tracks. Moreover, several studies indicate that APP processing may occur within axonal or presinaptic terminals, supporting the hypothesis that APP functions as a vesicular receptor for cytoskeletal motor proteins. In the current study, we test the hypothesis that myosin II, important contributor to the cytoskeleton of neuronal cells, may influence the trafficking and/or the processing of APP. Our results demonstrate that down-regulation of myosin II-B, the major myosin isoform in neurons, is able to increase AA secretion, concomitantly altering the subcellular localization of APP. These new insights might be important for the understanding of the function of APP and provide a novel conceptual framework in which to analyze its pathological role. Work funded by grants from COFIN 2004 (no. 2004068928_003 and no. 2004063943_001).
American Journal of Veterinary Research, 2009
Objective-To evaluate the use of a commercially available 5-carboxyfluorescein-based, intramolecu... more Objective-To evaluate the use of a commercially available 5-carboxyfluorescein-based, intramolecularly quenched, fluorescence resonance energy transfer (FRET) peptide substrate of renin for measurement of plasma renin concentration in cats. Sample Population-Plasma samples obtained during a previous study of renal autograft ischemia-reperfusion injury in 10 cats and samples of fetal bovine serum containing recombinant human renin (rh-renin). Procedures-Experiments involving samples of fetal bovine serum containing rh-renin were conducted to identify a suitable control vehicle, optimal substrate concentration, and appropriate duration of incubation. With the use of the identified assay conditions, a standard curve was constructed to allow conversion of relative fluorescent units into values of renin concentration (ng/mL). Subsequently, plasma samples obtained from cats before and after renal autograft ischemia-reperfusion injury were assayed to determine endogenous renin concentration. Results-Under conditions of a 1:50 substrate dilution and 4-hour incubation period, the assay detected small amounts of rh-renin in fetal bovine serum. A linear relationship (R 2 = 0.996) between the relative fluorescent units generated and exogenous rh-renin concentration was evident. The assay detected renin in plasma samples obtained from cats after renal autograft ischemia-reperfusion, and renin concentrations on days 1 and 2 after transplant differed significantly. Conclusions and Clinical Relevance-The study data indicated that the assay involving the FRET peptide substrate of renin is potentially a rapid and specific method for measurement of plasma renin concentration in cats.
Retrovirology, Jan 15, 2013
Previously, we reported the conversion of the 12-mer linear and cell-impermeable peptide CAI to a... more Previously, we reported the conversion of the 12-mer linear and cell-impermeable peptide CAI to a cell-penetrating peptide NYAD-1 by using an i,i + 4 hydrocarbon stapling technique and confirmed its binding to the C-terminal domain (CTD) of the HIV-1 capsid (CA) protein with an improved affinity (K(d) ~ 1 μM) compared to CAI (K(d) ~ 15 μM). NYAD-1 disrupts the formation of both immature- and mature-like virus particles in in vitro and cell-based assembly assays. In addition, it displays potent anti-HIV-1 activity in cell culture against a range of laboratory-adapted and primary HIV-1 isolates. In this report, we expanded the study to i,i + 7 hydrocarbon-stapled peptides to delineate their mechanism of action and antiviral activity. We identified three potent inhibitors, NYAD-36, -66 and -67, which showed strong binding to CA in NMR and isothermal titration calorimetry (ITC) studies and disrupted the formation of mature-like particles. They showed typical α-helical structures and pen...
Journal of Molecular Biology, 2008
Advances in Experimental Medicine and Biology, 2009
SARS-CoV-2 uses human angiotensin-converting enzyme 2 (ACE2) as the primary receptor to enter hos... more SARS-CoV-2 uses human angiotensin-converting enzyme 2 (ACE2) as the primary receptor to enter host cells and initiate the infection. The critical binding region of ACE2 is a ∼30 aa long helix. Here we report the design of four stapled peptides based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection. All stapled peptides showed high helical contents (50-94% helicity). On the contrary, the linear control peptide NYBSP-C showed no helicity (19%). We have evaluated the peptides in a pseudovirus based single-cycle assay in HT1080/ACE2 and human lung cells A549/ACE2, overexpressing ACE2. Three of the four stapled peptides showed potent antiviral activity in HT1080/ACE2 (IC50: 1.9 – 4.1 µM) and A549/ACE2 cells (IC50: 2.2 – 2.8 µM). The linear peptides NYBSP-C and the double-stapled peptide StRIP16, used as controls, showed no antiviral activity. Most significantly, none of the stapled peptides show...
Med. Chem. Commun., 2016
Herein, we describe the design and synthesis of a novel BODIPY-labelled minihepcidin peptide to e... more Herein, we describe the design and synthesis of a novel BODIPY-labelled minihepcidin peptide to enable the high content analysis of ferroportin (SLC40A1) pharmacology.
The Faseb Journal, Mar 1, 2008
The Faseb Journal, Apr 1, 2009
Bioorganic & Medicinal Chemistry, 2015
One of the most critical requirements of the infection of the human immunodeficiency virus type 1... more One of the most critical requirements of the infection of the human immunodeficiency virus type 1 (HIV-1) is the interaction of its surface envelope glycoprotein gp120 with the cellular receptor CD4, which initiates virus entry to cells. Therefore, envelope glycoprotein gp120 has been validated as a potential target to develop HIV-1 entry inhibitors. Here we report the evaluation of a novel non-natural amino acid, termed 882376, reported earlier as a precursor of a CD4-mimetic miniprotein, as HIV-1 entry inhibitor. 882376 showed HIV-1 inhibitory activity against a large panel of primary isolates of different subtype. Moreover, genotyping of 882376 resistant HIV-1 virus revealed three amino acid substitutions in the gp120 including one in the CD4 binding site suggesting that this molecule may bind to gp120 and prevent its binding to CD4. Additional neutralization experiments indicate that 882376 is not active against mutant pseudoviruses carrying the amino acid substitutions S375H and S375Y located in the 'Phe43 cavity' which is the major site of CD4 binding, suggesting that this compound may interfere with the interaction between gp120 and CD4. The unnatural amino acid, 882376, is expected to serve as a lead for further optimization to more potent HIV-1 entry inhibitors.
Peptides: The Wave of the Future, 2001
Peptides Across the Pacific: The Proceedings of the Twenty-Third American and the Sixth International Peptide Symposium, 2013
We extend to you a warm and sunny Aloha in celebration of the 23 rd American Peptide Symposium an... more We extend to you a warm and sunny Aloha in celebration of the 23 rd American Peptide Symposium and the 6 th International Symposium. The meeting theme, Peptides Across the Pacific, embraced the spirit of the scientific and social program. Peptides Across the Pacific encompassed the important role that peptide science currently plays in so many disciplines and explored the potential impact peptides can make in scientific fields that have yet to realize the utility of these wonderful molecules. The scientific program for 2013 was framed by distinguished lectures delivered by two renowned peptide chemists.