AI Article Synopsis
- Many biomaterials can adjust to changes in their biological environment, impacting their function and how they deliver substances.
- The adaptation process starts on a local structural level and moves up to larger molecular scales, highlighting the importance of understanding these fast structural changes for designing effective biomaterials.
- In this study, researchers used time-resolved X-ray scattering to investigate the structural dynamics of poly-l-glutamic acid when it reacts to a sudden change in pH, revealing important changes in peptide chain packing and structure formation.
Article Abstract
Many biomaterials can adapt to changes in the local biological environment (such as pH, temperature, or ionic composition) in order to regulate function or deliver a payload. Such adaptation to environmental perturbation is typically a hierarchical process that begins with a response at a local structural level and then propagates to supramolecular and macromolecular scales. Understanding fast structural dynamics that occur upon perturbation is important for rational design of functional biomaterials. However, few nanosecond time-resolved methods can probe both intra- and intermolecular scales simultaneously with a high structural resolution. Here, we utilize time-resolved X-ray scattering to probe nanosecond to microsecond structural dynamics of poly-l-glutamic acid undergoing protonation via a pH jump initiated by photoexcitation of a photoacid. Our results provide insights into the protonation-induced hierarchical changes in packing of peptide chains, formation of a helical structure, and the associated collapse of the peptide chain.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6533112 | PMC |
| http://dx.doi.org/10.1021/acs.jpcb.9b00072 | DOI Listing |
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