Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein
Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group...
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ftpubmed:oai:pubmedcentral.nih.gov:3509122 2023-05-15T14:01:32+02:00 Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein Shah, Syed Hussinien H. Kar, Rajiv K. Asmawi, Azren A. Rahman, Mohd Basyaruddin A. Murad, Abdul Munir A. Mahadi, Nor M. Basri, Mahiran Rahman, Raja Noor Zaliha A. Salleh, Abu B. Chatterjee, Subhrangsu Tejo, Bimo A. Bhunia, Anirban 2012-11-28 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509122 http://www.ncbi.nlm.nih.gov/pubmed/23209600 https://doi.org/10.1371/journal.pone.0049788 en eng Public Library of Science http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509122 http://www.ncbi.nlm.nih.gov/pubmed/23209600 http://dx.doi.org/10.1371/journal.pone.0049788 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. CC-BY Research Article Text 2012 ftpubmed https://doi.org/10.1371/journal.pone.0049788 2013-09-04T16:31:05Z Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities. Text Antarc* Antarctic Antarctica PubMed Central (PMC) Antarctic The Antarctic PLoS ONE 7 11 e49788 |
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Research Article Shah, Syed Hussinien H. Kar, Rajiv K. Asmawi, Azren A. Rahman, Mohd Basyaruddin A. Murad, Abdul Munir A. Mahadi, Nor M. Basri, Mahiran Rahman, Raja Noor Zaliha A. Salleh, Abu B. Chatterjee, Subhrangsu Tejo, Bimo A. Bhunia, Anirban Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
topic_facet |
Research Article |
description |
Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities. |
format |
Text |
author |
Shah, Syed Hussinien H. Kar, Rajiv K. Asmawi, Azren A. Rahman, Mohd Basyaruddin A. Murad, Abdul Munir A. Mahadi, Nor M. Basri, Mahiran Rahman, Raja Noor Zaliha A. Salleh, Abu B. Chatterjee, Subhrangsu Tejo, Bimo A. Bhunia, Anirban |
author_facet |
Shah, Syed Hussinien H. Kar, Rajiv K. Asmawi, Azren A. Rahman, Mohd Basyaruddin A. Murad, Abdul Munir A. Mahadi, Nor M. Basri, Mahiran Rahman, Raja Noor Zaliha A. Salleh, Abu B. Chatterjee, Subhrangsu Tejo, Bimo A. Bhunia, Anirban |
author_sort |
Shah, Syed Hussinien H. |
title |
Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
title_short |
Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
title_full |
Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
title_fullStr |
Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
title_full_unstemmed |
Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein |
title_sort |
solution structures, dynamics, and ice growth inhibitory activity of peptide fragments derived from an antarctic yeast protein |
publisher |
Public Library of Science |
publishDate |
2012 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509122 http://www.ncbi.nlm.nih.gov/pubmed/23209600 https://doi.org/10.1371/journal.pone.0049788 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509122 http://www.ncbi.nlm.nih.gov/pubmed/23209600 http://dx.doi.org/10.1371/journal.pone.0049788 |
op_rights |
This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1371/journal.pone.0049788 |
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PLoS ONE |
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7 |
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11 |
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e49788 |
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1766271377196711936 |