syed moin - Academia.edu (original) (raw)

Papers by syed moin

Cathelicidins are a group of oral antimicrobial peptides that play multiple vital roles in the hu... more Cathelicidins are a group of oral antimicrobial peptides that play multiple vital roles in the human body, such as their antimicrobial (broad spectrum) role against oral microbes, wound healing, and angiogenesis, with recent evidences about their role in cancer regulation. Cathelicidins are present in humans and other mammals as well. By complex interactions with the microenvironment, it results in pro-inflammatory effects. Many in vitro and in vivo experiments have been conducted to ultimately conclude that these unique peptides play an essential role in innate immunity. Peptides are released in the precursor form (defensins), which after cleavage results in cathelicidins formation. Living in the era where the major focus is on non-invasive and nanotechnology, this ultimately leads to further advancements in the field of salivaomics. Based on current spotlight innovations, we have highlighted the biochemistry, mode of action, and the importance of cathelicidins in the oral cavity.

The amino acid sequence of b I-globin chain from Sindhi Krait (Bungarus sindanus sindanus) was de... more The amino acid sequence of b I-globin chain from Sindhi Krait (Bungarus sindanus sindanus) was determined to study the molecular evolution among snakes. The hemoglobin was isolated from the red blood cells and was analyzed by ion-exchange chromatography (IEX). The crude globin was subjected to reversed phased-high performance liquid chromatography (RP-HPLC) using C4 column. The N-terminal sequences of intact globin chains and tryptic peptides were determined by Edman degradation in a pulsed liquid gas phase sequencer using an online Phenylthiohydantoin analyzer. Sindhi Krait is expected to express three hemoglobin components that are composed of b II , b I , a D and a A-globin chains, as apparent by IEX, RP-HPLC and N-terminal sequence analyses. Sequence alignment and phylogenetic analyses of b I globin chain from Sindhi Krait showed closest relationship with b I globin chain from Rattlesnake, Water snake and Indigo snake. Interestingly, comparison of primary sequence of b I globin chain of Sindhi Krait with human b chain revealed 63 % similarity along with the retention of all heme contact points. Variations among the two sequences were prominent at ab contact points and in regions directly not important for function.

A Phospholipase A 2 termed as BSS PLA 2 was purified from the venom of Bungarus sindanus sindanus... more A Phospholipase A 2 termed as BSS PLA 2 was purified from the venom of Bungarus sindanus sindanus (Sindhi Krait) through two steps: size exclusion chromatography on sephadex G-75 and reversed-phase chromatography on Vydac C18 HPLC column. The homogeneity and molecular mass of BSS PLA 2 were analysed by SDS-PAGE and MALDI-TOF mass spectrometry. The N-terminal sequence of 32 amino acids of the BSS PLA 2 revealed close resemblance with other species of bungarus snakes. The BSS PLA 2 showed an optimum activity in the alkaline range (pH 8.0-9.5), while the optimum temperature stability was found to be 60 °C. The effect of calcium ion (Ca 2+) concentration revealed that in the absence of Ca 2+ the enzyme showed some activity however, the enzymatic activity increases with increase in Ca 2+ concentration. The addition of exogenous metal ions, including Mg 2+ with Ca 2+ increases, while that of Ba 2+ with Ca 2+ slightly decreases the enzymatic activity of BSS PLA 2. Additionally, kappa bungarotoxin with the mass of 7358.5 Da was identified by MALDI TOF MS/MS from another peak of the same HPLC elution. Two of the tryptic peptides matched with kappa-6-bungarotoxin when searched through Mascot search engine.

Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen ... more Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Here we briefly discuss the purification, catalytic mechanism in light of available understanding of structure-function relationship and the tailoring side of the protein, which has been the subject of recent research. Purification strategy of laccases is a method of choice and is facilitated by increased production of the enzyme. The structure-function relationship has given insights to unfold the catalytic mechanism. Site directed mutagenesis and other modification at C-terminal end or surrounding environment of copper centres have shown promising results to fit for purpose aspect, with a lot remains to be explored in glycosylation status and its alteration.

In recent years, artemisinin (1) has remained an effective drug to treat malaria. Numerous approa... more In recent years, artemisinin (1) has remained an effective drug to treat malaria. Numerous approaches have been adapted to increase the efficacy of (1) against antibiotic resistant malarial parasite. Microbial biotransformation of (1) has been used recently to produce promising derivatives of (1) on a large scale with low costs. During the last decade several biotransformation studies on (1), by using microorganisms, have been reported. This literature review focuses on the most recent microbial transformation studies on artemisinin and its derivatives. INTRODUCTION Biotransformation involves the chemical transformation of substrates to desired products by using enzymes, either purified or crude, from microorganisms (bacteria and fungus), plants or animals [1,2]. Transformation of compounds by the application of whole cell microorganisms is often advantageous as compared to isolated enzymes [3]. These days, microbial transformation is considered to be the inexpensively and ecologically competitive technology for the biotechnological specialists in looking for new methods to produce pure useful chemicals, pharmaceutical, and agrochemical compounds [4]. Microbial transformation has been extensively used, to create new and useful metabolites of almost all classes of terpenes, as a substitute of chemical synthesis for preparation of pharmacologically active compounds [3]. The current review focuses on the microbial transformation of artemisnin (1) during the recent time. Scifinder research tool was used to screen the literature of this related subject, and to the best of our knowledge, this is the first review about the microbial biotransformation of (1).

Oral cancer refers to malignancies that have higher morbidity and mortality rates due to the late... more Oral cancer refers to malignancies that have higher morbidity and mortality rates due to the late stage diagnosis and no early detection of a reliable diagnostic marker, while oral squamous cell carcinoma (OSCC) is amongst the world's top ten most common cancers. Diagnosis of cancer requires highly sensitive and specific diagnostic tools which can support untraceable hidden sites of OSCC, yet to be unleashed, for which plenty of biomarkers are identified; the most recommended biomarker detection medium for OSCC includes biological fluids, such as blood and saliva. Saliva holds a promising future in the search for new clinical biomarkers that are easily accessible, less complex, accurate, and cost effective as well as being a non-invasive technique to follow, by analysing the malignant cells' molecular pathology obtained from saliva through proteomic, genomic and transcriptomic approaches. However, protein biomarkers provide an immense potential for developing novel marker-based assays for oral cancer, hence this current review offers an overall focus on the discovery of a panel of candidates as salivary protein biomarkers, as well as the proteomic tools used for their identification and their significance in early oral cancer detection.

Lignin is an important constitute of the wood and thus the organism like fungi and insects growin... more Lignin is an important constitute of the wood and thus the organism like fungi and insects growing on wood produce some extracellular lignolytic enzymes. In fungi these enzymes include different oxidases and peroxidases. Lignin peroxidases, manganese peroxidases, versatile peroxidases and laccases have been characterised from fungi and their roles in wood decay has been established. Here we report ABTS-oxidases from an unidentified fungus isolated from tree bark sample from Kuantan, Malaysia. After the liquid media cultivation, the crude extracellular protein content was extracted and analysed by polyacrylamide gel electrophoresis. SDS-PAGE, native PAGE and zymography were carried out. Azo dyes, brilliant green, trypan blue, direct red 80 and eriochrome black T were used for decolourisation activity of the isolated fungus on solid medium. The results suggest that the extracellular proteins contain laccase enzyme activity. Out of the four azo dyes that were used for dye decolourisation assay, at least three were decolourised to different extents by the fungus.

There are many human oral antimicrobial peptides responsible for playing important roles includin... more There are many human oral antimicrobial peptides responsible for playing important roles including maintenance, repairing of oral tissues (hard or soft) and defense against oral microbes. In this review we have highlighted the biochemistry, physiology and proteomics of human oral histatin peptides, secreted from parotid and submandibular salivary glands in human. The significance of these peptides includes capability for ionic binding that can kill fungal Candida albicans.