Literature DB >> 21727967

Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers.

Xingfei Zhou1, Jingsong Liu, Bin Li, Saju Pillai, Dongdong Lin, Jianhua Liu, Yi Zhang.   

Abstract

The process of glucagon peptide aggregation was studied with high resolution atomic force microscopy (AFM). The statistical analysis of ex situ AFM images in combination with in situ AFM observation suggests that it is more likely that (proto)fibrils are formed via direct longitudinal growth of oligomers, instead of the lateral association of two or more filaments. This journal is © The Royal Society of Chemistry 2011

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Year:  2011        PMID: 21727967     DOI: 10.1039/c1nr10332f

Source DB:  PubMed          Journal:  Nanoscale        ISSN: 2040-3364            Impact factor:   7.790


  2 in total

1.  Structural transitions and interactions in the early stages of human glucagon amyloid fibrillation.

Authors:  Balakrishnan S Moorthy; Hamed Tabatabaei Ghomi; Markus A Lill; Elizabeth M Topp
Journal:  Biophys J       Date:  2015-02-17       Impact factor: 4.033

2.  Self-assembly mechanisms of nanofibers from peptide amphiphiles in solution and on substrate surfaces.

Authors:  Hsien-Shun Liao; Jing Lin; Yang Liu; Peng Huang; Albert Jin; Xiaoyuan Chen
Journal:  Nanoscale       Date:  2016-08-04       Impact factor: 7.790

  2 in total

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