Interaction of class A amphipathic helical peptides with phospholipid unilamellar vesicles
The exchangeable apolipoproteins are important in determining the structure/function properties of lipoproteins. These proteins typically contain varying amounts of amphipathic helices. Five model peptides, 18A, Ac-18A-NH2, Ac-18R-NH2, 37pA, and 37aA, have been designed to investigate variations of...
Main Authors: | J A Gazzara, M C Phillips, S Lund-Katz, M N Palgunachari, J P Segrest, G M Anantharamaiah, J W Snow |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
1997-10-01
|
Series: | Journal of Lipid Research |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520371431 |
Similar Items
-
Effect of vesicle size on their interaction with class A amphipathic helical peptides
by: J A Gazzara, et al.
Published: (1997-10-01) -
Probing structure and function of VLDL by synthetic amphipathic helical peptides
by: B H Chung, et al.
Published: (1996-05-01) -
Computer programs to identify and classify amphipathic alpha helical domains.
by: MK Jones, et al.
Published: (1992-02-01) -
Effects of increasing hydrophobicity on the physical-chemical and biological properties of a class A amphipathic helical peptide
by: Geeta Datta, et al.
Published: (2001-07-01) -
Investigation of Unilamellar Phospholipid Vesicle Interactions with PNIPAM Based Hydrogel Beads
by: MacKinnon, Neil J.
Published: (2009)