title: Understanding Peptide Oligomeric State in Langmuir Monolayers of Amphiphilic 3-Helix Bundle-Forming Peptide-PEG Conjugates.
abstract: Coiled-coil peptide-polymer conjugates are an emerging class of biomaterials. Fundamental understanding of the coiled-coil oligomeric state and assembly process of these hybrid building blocks is necessary to exert control over their assembly into well-defined structures. Here, we studied the effect of peptide structure and PEGylation on the self-assembly process and oligomeric state of a Langmuir monolayer of amphiphilic coiled-coil peptide-polymer conjugates using X-ray reflectivity (XR) and grazing-incidence X-ray diffraction (GIXD). Our results show that the oligomeric state of PEGylated amphiphiles based on 3-helix bundle-forming peptide is surface pressure dependent, a mixture of dimers and trimers was formed at intermediate surface pressure but transitions into trimers completely upon increasing surface pressure. Moreover, the interhelical distance within the coiled-coil bundle of 3-helix peptide-PEG conjugate amphiphiles was not perturbed under high surface pressure. Present studies provide valuable insights into the self-assembly process of hybrid peptide-polymer conjugates and guidance to develop biomaterials with controlled multivalency of ligand presentation.
authors: Department of Materials Science and Engineering, University of California, Berkeley 94720, United States.|Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley 94720, United States.
authors: Reidar
authors: R
authors: Lund
authors: Department of Materials Science and Engineering, University of California, Berkeley 94720, United States.
authors: JooChuan
authors: J
authors: Ang
authors: Department of Materials Science and Engineering, University of California, Berkeley 94720, United States.
authors: Jessica Y
authors: JY
authors: Shu
authors: Department of Materials Science and Engineering, University of California, Berkeley 94720, United States.|Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley 94720, United States.|Department of Chemistry, University of California, Berkeley 94720, United States.
authors: Ting
authors: T
authors: Xu
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008962:Models, Theoretical; D010446:Peptide Fragments / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013501:Surface-Active Agents; D014961:X-Ray Diffraction
chemical_list: D001672:Biocompatible Materials; D008051:Lipid Bilayers; D010446:Peptide Fragments; D011108:Polymers; D013501:Surface-Active Agents; D011092:Polyethylene Glycols