Supramolecular assembly of Cp1-11 peptide and insulin for rapid-acting formulation
Year: 2017
Type: article
Abstract: In order to improve the life quality of diabetic patients, it is very important to develop rapid-acting insulin formulations that can mimic the physiological meal-time secretion profile of insulin in healthy people. Although several insulin analogues have been designed to provide postprandial glycemic control, still there are some serious disadvantages. A supramolecular strategy is presented here to inhibit insulin aggregation and improve its bioactivity by using Cp1-11 peptide. As a fragment of C-peptide in proinsulin, Cp1-11 peptide was found to influence insulin oligomerization by supramolecular interactions. This work demonstrates that the Cp1-11 peptide can interact with oligomeric insulin and facilitate its disaggregation into the physiologically active monomeric form. Computer simulation indicates that Cp1-11 can insert into the space between the C-terminal tail and the N-terminal helix of the B-chain of insulin, causing dissociation of the insulin dimer. The supramolecular assembly of Cp1-11 and insulin can improve the bioavailability and therapeutic effect of insulin on the control of in vivo blood glucose levels. These results suggest that Cp1-11 peptide can modulate the intermolecular interaction of aggregated insulin and prevent the transition from monomeric to multimeric states, and shows great potential for the development of an effective rapid-acting strategy to treat diabetes.
Authors: Weigang Wang, Sheyu Li, Zhouxiang Zhao, Anna Zhou, Yanpeng Liu, Yantao Chen, Mingchang Lin, Guosong Chen, Chunmei Ding, Jianshu Li
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: diamond
OpenAlex ID: W2745979183