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An investigation of the effect of se...

Salamat-Miller, Nazila.

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An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption.

Record Type:	Electronic resources : Monograph/item
Title/Author:	An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption./
Author:	Salamat-Miller, Nazila.
Description:	149 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0118.
Contained By:	Dissertation Abstracts International65-01B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118829

An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption.
Salamat-Miller, Nazila.

An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption. - 149 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0118.

Thesis (Ph.D.)--University of Missouri - Kansas City, 2004.

The objective of the current research was to investigate how the secondary structure of a polypeptide affects its diffusion in the aqueous-filled paracellular route of a membrane. Polypeptides, in the absence of tertiary structure, exhibit different conformations such as random coil (RC), alpha helix (alpha-helix), or beta sheet (beta) secondary structures. Exhibition of different conformations results in the formation of polypeptides with different overall molecular dimensions such as increased flexibility of a random coil compared to an alpha-helix or a beta structure, and specific molecular properties including different diffusitive properties. The RC conformation usually forms an irregular coiled chain with free movement in the solution, while an alpha-helix arrangement resembles a rod with less flexibility. The beta conformation forms an elongated and pleated sheet with low aqueous solubility properties. The general purpose of the current research was to investigate the relationship between the overall molecular geometry, directly conferred by a polypeptide's secondary conformation, to its hindered and unhindered diffusional properties in solution, in the hope of identifying key factors governing the paracellular absorption for this class of therapeutics. The paracellular route is a viable pathway for the diffusion of polypeptides across biological membranes. A survey of the literature on parameters affecting paracellular transport of polypeptides and proteins demonstrates the lack of a systematic study of the influence of three-dimensional structure/secondary structure of polypeptides on their diffusion in vitro and absorption in vivo. In the present research, the following investigations were conducted; (1) permeation of Conantokin G across a microporous cellulose ester membrane in vitro , (2) permeation of the synthetic model polypeptides across a microporous polyester membrane in vitro, and (3) diffusion of the synthetic model polypeptides across a biological membrane in vitro (Caco-2 cell monolayer) and their absorption in situ.Subjects--Topical Terms:

1019105
Biophysics, General.

An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption.
LDR:03242nmm 2200277 4500 001 1865029
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035 $a (UnM)AAI3118829
035 $a AAI3118829
040 $a UnM $c UnM
100 1 $a Salamat-Miller, Nazila. $3 1952492
245 1 3 $a An investigation of the effect of secondary structure of model polypeptides on their in vitro diffusion and in situ absorption.
300 $a 149 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0118.
500 $a Adviser: Thomas P. Johnston.
502 $a Thesis (Ph.D.)--University of Missouri - Kansas City, 2004.
520 $a The objective of the current research was to investigate how the secondary structure of a polypeptide affects its diffusion in the aqueous-filled paracellular route of a membrane. Polypeptides, in the absence of tertiary structure, exhibit different conformations such as random coil (RC), alpha helix (alpha-helix), or beta sheet (beta) secondary structures. Exhibition of different conformations results in the formation of polypeptides with different overall molecular dimensions such as increased flexibility of a random coil compared to an alpha-helix or a beta structure, and specific molecular properties including different diffusitive properties. The RC conformation usually forms an irregular coiled chain with free movement in the solution, while an alpha-helix arrangement resembles a rod with less flexibility. The beta conformation forms an elongated and pleated sheet with low aqueous solubility properties. The general purpose of the current research was to investigate the relationship between the overall molecular geometry, directly conferred by a polypeptide's secondary conformation, to its hindered and unhindered diffusional properties in solution, in the hope of identifying key factors governing the paracellular absorption for this class of therapeutics. The paracellular route is a viable pathway for the diffusion of polypeptides across biological membranes. A survey of the literature on parameters affecting paracellular transport of polypeptides and proteins demonstrates the lack of a systematic study of the influence of three-dimensional structure/secondary structure of polypeptides on their diffusion in vitro and absorption in vivo. In the present research, the following investigations were conducted; (1) permeation of Conantokin G across a microporous cellulose ester membrane in vitro , (2) permeation of the synthetic model polypeptides across a microporous polyester membrane in vitro, and (3) diffusion of the synthetic model polypeptides across a biological membrane in vitro (Caco-2 cell monolayer) and their absorption in situ.
520 $a The present investigation demonstrates the importance of the secondary structure of a polypeptide on its free diffusion in vitro and the significance of its flexibility for hindered diffusion in vitro as well as in situ.
590 $a School code: 0134.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Health Sciences, Pharmacy. $3 1017737
690 $a 0786
690 $a 0572
710 2 0 $a University of Missouri - Kansas City. $3 1021712
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Johnston, Thomas P., $e advisor
790 $a 0134
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118829