APS March Meeting 2016
Volume 61, Number 2
Monday–Friday, March 14–18, 2016;
Baltimore, Maryland
Session P34: Biopolymers and Biohybrid Polymers - Assembly and Thermodynamics
2:30 PM–5:30 PM,
Wednesday, March 16, 2016
Room: 337
Sponsoring
Unit:
DPOLY
Chair: Muzhou Wang, NIST
Abstract ID: BAPS.2016.MAR.P34.10
Abstract: P34.00010 : Tuning the entropic spring to dictate order and functionality in polymer conjugated peptide biomaterials
4:18 PM–4:54 PM
Preview Abstract
Abstract
Author:
Sinan Keten
(Northwestern University)
Hybrid peptide-polymer conjugates have the potential to combine the
advantages of natural proteins and synthetic polymers, resulting in
biomaterials with improved stability, controlled assembly, and tailored
functionalities. However, the effect of polymer conjugation on peptide
structural organization and functionality, along with the behavior of
polymers at the interface with biomolecules remain to be fully understood.
This talk will summarize our recent efforts towards establishing a modeling
framework to design entropic forces in helix-polymer conjugates and
polymer-conjugated peptide nanotubes to achieve hierarchical self-assembling
systems with predictable order. The first part of the talk will discuss how
self-assembly principles found in biology, combined with polymer physics
concepts can be used to create artificial membranes that mimic certain
features of ion channels. Thermodynamics and kinetics aspects of
self-assembly and how it governs the growth and stacking sequences of
peptide nanotubes will be discussed, along with its implications for
nanoscale transport. The second part of the talk will review advances
related to modeling polymer conjugated coiled coils at relevant length and
time scales. Atomistic simulations combined with sampling techniques will be
presented to discuss the energy landscapes governing coiled-coil stability,
revealing cascades of events governing disassembly. This will be followed by
a discussion of mechanisms through which polymers can stabilize small
proteins, such as shielding of solvents, and how specific peptide sequences
can reciprocate by altering polymer conformations. Correlations between
mechanical and thermal stability of peptides will be discussed. Finally,
coarse-grained simulations will provide insight into how the location of
polymer attachment changes entropic forces and higher-level organization in
helix bundle assemblies. Our findings set the stage for a
materials-by-design capability towards dictating complex topologies of
polymer-peptide conjugate systems.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2016.MAR.P34.10