title: Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers.
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.
authors: Physical Department, Ningbo University, Ningbo Zhejiang, China. zhouxingfei@nbu.edu.cn
authors: Xingfei
authors: X
authors: Zhou
authors: Jingsong
authors: J
authors: Liu
authors: Bin
authors: B
authors: Li
authors: Saju
authors: S
authors: Pillai
authors: Dongdong
authors: D
authors: Lin
authors: Jianhua
authors: J
authors: Liu
authors: Yi
authors: Y
authors: Zhang
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D001669:Biochemical Phenomena; D005934:Glucagon / Q000737:chemistry / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure*; D058105:Polymerization
chemical_list: D000682:Amyloid; D005934:Glucagon