Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1

Organisms living in cold environment produce antifreeze proteins (AFPs) which exhibit special functions as a result of cold adaptation. AFP is currently being identified in many organisms such as bacteria, plants, fish, and fungi that are exposed to freezing stress. This study aimed to create novel...

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Main Author:	Said Amin Shah, Syed Hussinien Hielmie Shah
Format:	Thesis
Language:	English
Published:	2013
Subjects:	Antifreeze proteins
Online Access:	http://psasir.upm.edu.my/id/eprint/67359/1/FS%202013%2090%20IR.pdf
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id	my-upm-ir.67359
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spelling	my-upm-ir.673592019-03-12T01:20:35Z Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1 2013-07 Said Amin Shah, Syed Hussinien Hielmie Shah Organisms living in cold environment produce antifreeze proteins (AFPs) which exhibit special functions as a result of cold adaptation. AFP is currently being identified in many organisms such as bacteria, plants, fish, and fungi that are exposed to freezing stress. This study aimed to create novel antifreeze peptides based on the three-dimensional structure of Glaciozyma antarctica antifreeze protein-1 (AFP-1). Computational prediction on the structure of AFP-1 suggests that the helical segments of this protein are responsible for antifreeze activity. Six peptides derived from the sequence of G. antarctica have been synthesized. The peptides show measurable antifreeze activity as quantitatively measured by thermal hysteresis (TH) assay and qualitatively by ice recrystallization inhibition (IRI) assay. Structure determination of antifreeze peptides was carried out based on spectroscopic data obtained by using one dimensional and two dimensional 1H-NMR (800 MHz) in elucidating the structures of obtained peptides. All antifreeze peptides showed increase of thermal hysteresis value which is relative to the increase of antifreeze peptides concentration until the saturation point of solution. Peptide 1m recored the highest antifreeze activity with TH value 0.097 ± 0.004 oC, almost similar to the parent protein AFP-1 (0.1oC in concentration 0.1mM). Analysis of relationship between the peptide NMR structure and its activity showed that the peptides form alpha helical structure and the extent of peptide helicity greatly influences the activity of antifreeze peptides derived from G. antarctica AFP-1 segments. Antifreeze proteins 2013-07 Thesis http://psasir.upm.edu.my/id/eprint/67359/ http://psasir.upm.edu.my/id/eprint/67359/1/FS%202013%2090%20IR.pdf text en public masters Universiti Putra Malaysia Antifreeze proteins
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English
topic	Antifreeze proteins
spellingShingle	Antifreeze proteins Said Amin Shah, Syed Hussinien Hielmie Shah Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
description	Organisms living in cold environment produce antifreeze proteins (AFPs) which exhibit special functions as a result of cold adaptation. AFP is currently being identified in many organisms such as bacteria, plants, fish, and fungi that are exposed to freezing stress. This study aimed to create novel antifreeze peptides based on the three-dimensional structure of Glaciozyma antarctica antifreeze protein-1 (AFP-1). Computational prediction on the structure of AFP-1 suggests that the helical segments of this protein are responsible for antifreeze activity. Six peptides derived from the sequence of G. antarctica have been synthesized. The peptides show measurable antifreeze activity as quantitatively measured by thermal hysteresis (TH) assay and qualitatively by ice recrystallization inhibition (IRI) assay. Structure determination of antifreeze peptides was carried out based on spectroscopic data obtained by using one dimensional and two dimensional 1H-NMR (800 MHz) in elucidating the structures of obtained peptides. All antifreeze peptides showed increase of thermal hysteresis value which is relative to the increase of antifreeze peptides concentration until the saturation point of solution. Peptide 1m recored the highest antifreeze activity with TH value 0.097 ± 0.004 oC, almost similar to the parent protein AFP-1 (0.1oC in concentration 0.1mM). Analysis of relationship between the peptide NMR structure and its activity showed that the peptides form alpha helical structure and the extent of peptide helicity greatly influences the activity of antifreeze peptides derived from G. antarctica AFP-1 segments.
format	Thesis
qualification_level	Master's degree
author	Said Amin Shah, Syed Hussinien Hielmie Shah
author_facet	Said Amin Shah, Syed Hussinien Hielmie Shah
author_sort	Said Amin Shah, Syed Hussinien Hielmie Shah
title	Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
title_short	Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
title_full	Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
title_fullStr	Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
title_full_unstemmed	Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1
title_sort	structure and function of novel antifreeze peptides derived from glaciozyma antarctica antifreeze protein-1
granting_institution	Universiti Putra Malaysia
publishDate	2013
url	http://psasir.upm.edu.my/id/eprint/67359/1/FS%202013%2090%20IR.pdf
_version_	1747812462470627328

Structure and function of novel antifreeze peptides derived from Glaciozyma antarctica antifreeze protein-1

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