title: Amphiphilic peptide-polymer conjugates based on the coiled-coil helix bundle.
abstract: Amphiphilic peptide-polymer conjugates can lead to hierarchically structured, biomolecular materials. Because the peptide structure determines the size, shape, and intermolecular interactions of these building blocks, systematic understanding of how the peptide structure and functionality are affected upon implementing hydrophobicity is required to direct their assemblies in solution and in the solid state. However, depending on the peptide sequence and native structure, previous studies have shown that the hydrophobic moieties affect peptide structures differently. Here, we present a solution study of amphiphilic peptide-polymer conjugates, where a hydrophobic polymer, polystyrene, is covalently linked to the N-terminus of a coiled-coil helix bundle-forming peptide. The effect of conjugated hydrophobic polymers on the peptide secondary and tertiary structures was examined using two types of model, coiled-coil helix bundles. In particular, the integrity of the binding pocket within the helix bundle upon hydrophobic polymer conjugation was evaluated. Upon attachment of polystyrene to the peptide N-terminus, the coiled-coil helices partially unfolded and functionality within the bundle core was inhibited. These observations are attributed to favorable interactions between hydrophobic residues with the PS block at the peptide-polymer interface that lead to rearrangement of peptide residues and consequently, unfolding of peptide structures. Thus, the hydrophobicity of the covalently linked polymers modifies the conjugates' architecture, size, and shape and may be used to tailor the assembly and disassembly process. Furthermore, the hydrophobicity of the covalently linked polymer needs to be taken into consideration to maintain the built-in functionalities of protein motifs when constructing amphiphilic peptide-polymer conjugates.
authors.affiliation: Department of Materials Science and Engineering, University of California, Berkeley, California 94720, USA.
authors.forename: Jessica Y
authors.initials: JY
authors.lastname: Shu
authors.forename: Yu-Ja
authors.initials: YJ
authors.lastname: Huang
authors.forename: Cen
authors.initials: C
authors.lastname: Tan
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Presley
authors.forename: Joseph
authors.initials: J
authors.lastname: Chang
authors.forename: Ting
authors.initials: T
authors.lastname: Xu
mesh_terms: D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D008027:Light; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D011137:Polystyrenes / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013501:Surface-Active Agents / Q000737:chemistry*
chemical_list: D010455:Peptides; D011137:Polystyrenes; D013501:Surface-Active Agents; D011092:Polyethylene Glycols