Pasha Tabatabai, A.
, Weigandt, K.
and Blair, D.
(2017),
Acid-Induced Assembly of a Reconstituted Silk Protein System, Physical Review E, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=922542
(Accessed October 31, 2024)
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Acid-Induced Assembly of a Reconstituted Silk Protein System
Published
Author(s)
A. Pasha Tabatabai, , Daniel L. Blair
Abstract
The chemical reconstitution of silk cocoons into stable aqueous suspensions allows for the creation of new classes of strong, biocompatible, and biodegradable silk materials. The addition of < 8 mM hydrochloric acid to a reconstituted silk solution induces aggregation, while no structural changes occur in the presence of salt at the same concentrations. Aggregate formation is not correlated to protein protonation. We investigate the structures present on the protein and aggregate lengthscales in these solutions using both optical and neutron scattering, while mass spectroscopy techniques shed light on a possible mechanism for aggregate formation. We find that the introduction of acid modulates the aggregate size and pervaded volume of the protein, an effect that is not observed with salt.Citation
Physical Review E
Volume
96
Issue
2
Pub Type
Journals
Download Paper
Citation
Issues
If you have any questions about this publication or are having problems accessing it, please contact reflib@nist.gov.
Created August 9, 2017, Updated October 12, 2021