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Rational peptide design for function...

Rajagopal, Karthikan.

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Rational peptide design for functional materials via molecular self-assembly.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Rational peptide design for functional materials via molecular self-assembly./
Author:	Rajagopal, Karthikan.
Description:	235 p.
Notes:	Adviser: Joel P. Schneider.
Contained By:	Dissertation Abstracts International67-12B.
Subject:	Chemistry, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3247722

Rational peptide design for functional materials via molecular self-assembly.
Rajagopal, Karthikan.

Rational peptide design for functional materials via molecular self-assembly. - 235 p.

Adviser: Joel P. Schneider.

Thesis (Ph.D.)--University of Delaware, 2007.

Supra-molecular self-assembly of rationally designed peptides is a promising approach to construct functional materials. This thesis specifically focuses on hydrogels, an important class of materials with potential for applications in tissue engineering, drug delivery and micro-fluidic systems. The objective is to design short peptides that would specifically adopt a stimulus dependent conformation that is strongly amenable to self-assembly resulting in material formation. With this concept the rational design of a 20 amino acid peptide (MAX1) that folds into an amphiphilic beta-hairpin structure and then self-assembles to form a rigid hydrogel under alkaline conditions is presented. The molecular level conformation of MAX1 was characterized using circular dichroism and FTIR spectroscopies. The mesoscale structure of the hydrogel assessed using confocal and transmission electron micron microscopies and neutron scattering techniques shows that peptide self-assembly results in the formation of fibrils that are homogeneously 3 nm in diameter. The mechanical properties of the hydrogel probed using oscillatory rheology shows that MAX1 forms a stiff hydrogel. Since the self-assembly process is coupled to the intra-molecularly folded state of the peptide, stimulus responsiveness can be specifically engineered into the sequence by rational design. This was demonstrated in the design of peptides that form hydrogels in response to a specific stimulus such as temperature, pH or ionic strength.Subjects--Topical Terms:

1021807
Chemistry, General.

Rational peptide design for functional materials via molecular self-assembly.
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035 $a (UMI)AAI3247722
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100 1 $a Rajagopal, Karthikan. $3 1282211
245 1 0 $a Rational peptide design for functional materials via molecular self-assembly.
300 $a 235 p.
500 $a Adviser: Joel P. Schneider.
500 $a Source: Dissertation Abstracts International, Volume: 67-12, Section: B, page: 7049.
502 $a Thesis (Ph.D.)--University of Delaware, 2007.
520 $a Supra-molecular self-assembly of rationally designed peptides is a promising approach to construct functional materials. This thesis specifically focuses on hydrogels, an important class of materials with potential for applications in tissue engineering, drug delivery and micro-fluidic systems. The objective is to design short peptides that would specifically adopt a stimulus dependent conformation that is strongly amenable to self-assembly resulting in material formation. With this concept the rational design of a 20 amino acid peptide (MAX1) that folds into an amphiphilic beta-hairpin structure and then self-assembles to form a rigid hydrogel under alkaline conditions is presented. The molecular level conformation of MAX1 was characterized using circular dichroism and FTIR spectroscopies. The mesoscale structure of the hydrogel assessed using confocal and transmission electron micron microscopies and neutron scattering techniques shows that peptide self-assembly results in the formation of fibrils that are homogeneously 3 nm in diameter. The mechanical properties of the hydrogel probed using oscillatory rheology shows that MAX1 forms a stiff hydrogel. Since the self-assembly process is coupled to the intra-molecularly folded state of the peptide, stimulus responsiveness can be specifically engineered into the sequence by rational design. This was demonstrated in the design of peptides that form hydrogels in response to a specific stimulus such as temperature, pH or ionic strength.
520 $a The significance of peptide design in the context of self-assembly and its relationship to the nanostructure was studied by designing a series of peptides derived from MAX1. Evolving from these studies is an understanding of the relationship between molecular level peptide structure and the nanoscale supra-molecular morphology. Based on this, it has been shown that alternate morphologies distinct from those observed with the gel forming peptides, such as non-twisting laminates or tube-like structures can be constructed. Lastly, it is shown that within amphiphilic beta-hairpin peptides, the turn sequence can be used as a design element to control the stiffness of the hydrogel which is an important property from an application point of view. These studies demonstrate that rationally designed peptides are robust building blocks to construct functional materials via molecular self-assembly.
590 $a School code: 0060.
650 4 $a Chemistry, General. $3 1021807
650 4 $a Engineering, Materials Science. $3 1017759
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773 0 $t Dissertation Abstracts International $g 67-12B.
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790 1 0 $a Schneider, Joel P., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3247722