The effects of ionic strength and pH on self-assembly of peptide

Self-coacervation of peptides is a spontaneous liquid-liquid phase separation triggered by the non-covalent interactions between peptide molecules. The coacervation behaviours can be regulated by both internal and external stimuli. The project aims to investigate the parameters, which are the ionic...

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Main Author: Zhu, Yinqi
Other Authors: Yu Jing
Format: Final Year Project
Language:English
Published: Nanyang Technological University 2023
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Online Access:https://hdl.handle.net/10356/166705
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1667052023-05-27T16:46:03Z The effects of ionic strength and pH on self-assembly of peptide Zhu, Yinqi Yu Jing School of Materials Science and Engineering yujing@ntu.edu.sg Engineering::Materials::Biomaterials Self-coacervation of peptides is a spontaneous liquid-liquid phase separation triggered by the non-covalent interactions between peptide molecules. The coacervation behaviours can be regulated by both internal and external stimuli. The project aims to investigate the parameters, which are the ionic strength, pH, and composition of peptide GG23, that affect the coacervation of the peptide. The effect of ionic strength on self-coacervation was evaluated by altering the concentration of sodium chloride in the peptide-salt solution. And the pH effect on the coacervation was revealed by dissolving peptide powder in two buffer solutions with different pH values. To investigate the effect of the peptide composition on self-coacervation, the peptide GG23K was prepared by substituting lysine (Lys) residues for aspartic acid (Asp) residues in GG23. The coacervates formed under different conditions were investigated by the optical microscope. GG23 tends to form coacervates under low pH and high ionic strength conditions. And Lys residues in GG23K help to improve the capability of peptide self-coacervation. The results may be beneficial for controlling self-coacervation behaviours and designing self-coacervating peptides for biomedical applications. Further research can be carried out to investigate the precise pH range where coacervates can be formed and the effects of temperature on the peptide coacervation. Bachelor of Engineering (Materials Engineering) 2023-05-23T11:59:51Z 2023-05-23T11:59:51Z 2023 Final Year Project (FYP) Zhu, Y. (2023). The effects of ionic strength and pH on self-assembly of peptide. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/166705 https://hdl.handle.net/10356/166705 en application/pdf Nanyang Technological University
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Materials::Biomaterials
spellingShingle Engineering::Materials::Biomaterials
Zhu, Yinqi
The effects of ionic strength and pH on self-assembly of peptide
description Self-coacervation of peptides is a spontaneous liquid-liquid phase separation triggered by the non-covalent interactions between peptide molecules. The coacervation behaviours can be regulated by both internal and external stimuli. The project aims to investigate the parameters, which are the ionic strength, pH, and composition of peptide GG23, that affect the coacervation of the peptide. The effect of ionic strength on self-coacervation was evaluated by altering the concentration of sodium chloride in the peptide-salt solution. And the pH effect on the coacervation was revealed by dissolving peptide powder in two buffer solutions with different pH values. To investigate the effect of the peptide composition on self-coacervation, the peptide GG23K was prepared by substituting lysine (Lys) residues for aspartic acid (Asp) residues in GG23. The coacervates formed under different conditions were investigated by the optical microscope. GG23 tends to form coacervates under low pH and high ionic strength conditions. And Lys residues in GG23K help to improve the capability of peptide self-coacervation. The results may be beneficial for controlling self-coacervation behaviours and designing self-coacervating peptides for biomedical applications. Further research can be carried out to investigate the precise pH range where coacervates can be formed and the effects of temperature on the peptide coacervation.
author2 Yu Jing
author_facet Yu Jing
Zhu, Yinqi
format Final Year Project
author Zhu, Yinqi
author_sort Zhu, Yinqi
title The effects of ionic strength and pH on self-assembly of peptide
title_short The effects of ionic strength and pH on self-assembly of peptide
title_full The effects of ionic strength and pH on self-assembly of peptide
title_fullStr The effects of ionic strength and pH on self-assembly of peptide
title_full_unstemmed The effects of ionic strength and pH on self-assembly of peptide
title_sort effects of ionic strength and ph on self-assembly of peptide
publisher Nanyang Technological University
publishDate 2023
url https://hdl.handle.net/10356/166705
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