Conformation of alloHyp in the Y position in the host-guest peptide with the pro-pro-gly sequence: implication of the destabilization of (Pro-alloHyp-Gly)10 - PubMed (original) (raw)
. 2006 Feb 15;81(3):225-33.
doi: 10.1002/bip.20405.
Affiliations
- PMID: 16273514
- DOI: 10.1002/bip.20405
Conformation of alloHyp in the Y position in the host-guest peptide with the pro-pro-gly sequence: implication of the destabilization of (Pro-alloHyp-Gly)10
Nattha Jiravanichanun et al. Biopolymers. 2006.
Abstract
The crystal structure of the host-guest peptide, (Pro-Pro-Gly)4-(Pro-alloHyp-Gly)-(Pro-Pro-Gly)4, was analyzed at high resolution. allohydroxyproline (alloHyp), 4S-hydroxyproline, was successfully characterized through the use of a host-guest peptide, while the previous study indicated the inability of a triple helical formation of (Pro-alloHyp-Gly)10. A detailed analysis of alloHyp conformation in collagen-like models sheds light on the role played by its puckering in the triple-helix stabilization and destabilization. That is, the alloHyp typically adopts down puckering. However, it adopted up puckering in the Y position in the Pro-alloHyp-Gly guest triplet, which was not preferable conformation for alloHyp. Therefore, the energetically unfavorable conformations seemed to play the key role in giving destabilization to the triple helix in (Pro-alloHyp-Gly)10. The intrinsic hydration pattern in (Pro-Pro-Gly)9 was conserved even in the surrounding alloHyp residues.
Copyright (c) 2005 Wiley Periodicals, Inc.
Similar articles
- High-resolution structures of collagen-like peptides [(Pro-Pro-Gly)4-Xaa-Yaa-Gly-(Pro-Pro-Gly)4]: implications for triple-helix hydration and Hyp(X) puckering.
Okuyama K, Hongo C, Wu G, Mizuno K, Noguchi K, Ebisuzaki S, Tanaka Y, Nishino N, Bächinger HP. Okuyama K, et al. Biopolymers. 2009 May;91(5):361-72. doi: 10.1002/bip.21138. Biopolymers. 2009. PMID: 19137577 - Triple-helix propensity of hydroxyproline and fluoroproline: comparison of host-guest and repeating tripeptide collagen models.
Persikov AV, Ramshaw JA, Kirkpatrick A, Brodsky B. Persikov AV, et al. J Am Chem Soc. 2003 Sep 24;125(38):11500-1. doi: 10.1021/ja036673+. J Am Chem Soc. 2003. PMID: 13129344 - Unexpected puckering of hydroxyproline in the guest triplets, hyp-pro-gly and pro-allohyp-gly sandwiched between pro-pro-gly sequence.
Jiravanichanun N, Hongo C, Wu G, Noguchi K, Okuyama K, Nishino N, Silva T. Jiravanichanun N, et al. Chembiochem. 2005 Jul;6(7):1184-7. doi: 10.1002/cbic.200500055. Chembiochem. 2005. PMID: 15929160 No abstract available. - Triple-helical peptides: an approach to collagen conformation, stability, and self-association.
Brodsky B, Thiagarajan G, Madhan B, Kar K. Brodsky B, et al. Biopolymers. 2008 May;89(5):345-53. doi: 10.1002/bip.20958. Biopolymers. 2008. PMID: 18275087 Review. - Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides.
Ramshaw JA, Shah NK, Brodsky B. Ramshaw JA, et al. J Struct Biol. 1998;122(1-2):86-91. doi: 10.1006/jsbi.1998.3977. J Struct Biol. 1998. PMID: 9724608 Review.
Cited by
- Collagen-Derived Peptides in CKD: A Link to Fibrosis.
Mavrogeorgis E, Mischak H, Latosinska A, Vlahou A, Schanstra JP, Siwy J, Jankowski V, Beige J, Jankowski J. Mavrogeorgis E, et al. Toxins (Basel). 2021 Dec 23;14(1):10. doi: 10.3390/toxins14010010. Toxins (Basel). 2021. PMID: 35050988 Free PMC article. - Synthesis and biological applications of collagen-model triple-helical peptides.
Fields GB. Fields GB. Org Biomol Chem. 2010 Mar 21;8(6):1237-58. doi: 10.1039/b920670a. Epub 2010 Jan 20. Org Biomol Chem. 2010. PMID: 20204190 Free PMC article. Review. - Collagen structure and stability.
Shoulders MD, Raines RT. Shoulders MD, et al. Annu Rev Biochem. 2009;78:929-58. doi: 10.1146/annurev.biochem.77.032207.120833. Annu Rev Biochem. 2009. PMID: 19344236 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources