Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2004.

Bibliographic Details
Main Author: Yang, Steve J., 1976-
Other Authors: Alexander Rich and Shuguang Zhang.
Format: Thesis
Language:eng
Published: Massachusetts Institute of Technology 2006
Subjects:
Online Access:http://hdl.handle.net/1721.1/32251
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author Yang, Steve J., 1976-
author2 Alexander Rich and Shuguang Zhang.
author_facet Alexander Rich and Shuguang Zhang.
Yang, Steve J., 1976-
author_sort Yang, Steve J., 1976-
collection MIT
description Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2004.
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spelling mit-1721.1/322512019-04-09T17:31:09Z Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids Yang, Steve J., 1976- Alexander Rich and Shuguang Zhang. Massachusetts Institute of Technology. Dept. of Biology. Massachusetts Institute of Technology. Dept. of Biology. Biology. Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2004. Includes bibliographical references. Progress in biology has always been linked to the development of novel materials and techniques such as agar for bacterial culture, agarose for nucleic acid gel electrophoresis to new fluorescent molecules for microscopy. Invention of new tools is necessary for future solutions to biological problems. One such important problem is the study of membrane proteins, most of which are not amenable to biochemical or structural studies due to their inherent insolubility and instability outside of the natural cellular membrane. Here we describe the development and behavior of a new class of amphiphilic molecules made of peptides, which may be used for solubilization and stabilization of membrane proteins. The peptides have a hydrophilic head group and a hydrophobic tail and self-assemble in aqueous solution to form tubes, vesicles and membranes. Each monomer is around 7 or 8 amino acids in length, but longer or shorter molecules can be very easily synthesized using standard peptide synthesis protocols. Two general motifs of amphiphilic peptides were designed based on the identity of the head group: one has a phosphoserine and the other, aspartic acid. For the phosphoserine peptide, the self-assembling behavior was investigated at different pH, salt concentrations and temperature. The critical aggregation concentrations of both motifs were also investigated. It was discovered that after a certain concentration, the peptides aggregated into different structures, and this self-assembling behavior is dependent on the environmental conditions. by Steve J. Yang. Ph.D. 2006-03-29T18:27:44Z 2006-03-29T18:27:44Z 2004 2004 Thesis http://hdl.handle.net/1721.1/32251 56023381 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 227, [16] p. 10140231 bytes 10136386 bytes application/pdf application/pdf application/pdf Massachusetts Institute of Technology
spellingShingle Biology.
Yang, Steve J., 1976-
Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title_full Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title_fullStr Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title_full_unstemmed Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title_short Self-assembly of aurfactant-like amphiphilic peptides made of natural amino acids
title_sort self assembly of aurfactant like amphiphilic peptides made of natural amino acids
topic Biology.
url http://hdl.handle.net/1721.1/32251
work_keys_str_mv AT yangstevej1976 selfassemblyofaurfactantlikeamphiphilicpeptidesmadeofnaturalaminoacids