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

Xingfei Zhou; Jingsong Liu; Bin Li; S. Pillai; Dongdong Lin; Jianhua Liu; Yi Zhang

doi:10.1039/c1nr10332f

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

Xingfei Zhou, Jingsong Liu, Bin Li, S. Pillai, Dongdong Lin, Jianhua Liu, Yi Zhang

Solid and Computational Mechanics

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

10 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Nanoscale
Vol/bind	3
Udgave nummer	8
Sider (fra-til)	3049-3051
Antal sider	3
ISSN	2040-3364
DOI	https://doi.org/10.1039/c1nr10332f
Status	Udgivet - aug. 2011

Adgang til dokumentet

10.1039/c1nr10332f

AUB Link

Søg efter materialet i Aalborg Universitetsbiblioteks søgemaskine

Andre filer og links

Link to publication in Scopus

Citationsformater

@article{66069ad4469b427b8bb59164975a3a89,

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.",

author = "Xingfei Zhou and Jingsong Liu and Bin Li and S. Pillai and Dongdong Lin and Jianhua Liu and Yi Zhang",

year = "2011",

month = aug,

doi = "10.1039/c1nr10332f",

language = "English",

volume = "3",

pages = "3049--3051",

journal = "Nanoscale",

issn = "2040-3364",

publisher = "Royal Society of Chemistry",

number = "8",

}

TY - JOUR

T1 - Assembly of glucagon (proto)fibrils by longitudinal addition of oligomers

AU - Zhou, Xingfei

AU - Liu, Jingsong

AU - Li, Bin

AU - Pillai, S.

AU - Lin, Dongdong

AU - Liu, Jianhua

AU - Zhang, Yi

PY - 2011/8

Y1 - 2011/8

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=80051598943&partnerID=8YFLogxK

U2 - 10.1039/c1nr10332f

DO - 10.1039/c1nr10332f

M3 - Journal article

AN - SCOPUS:80051598943

SN - 2040-3364

VL - 3

SP - 3049

EP - 3051

JO - Nanoscale

JF - Nanoscale

IS - 8

ER -

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

Abstract

Adgang til dokumentet

AUB Link

Andre filer og links

Fingeraftryk

Citationsformater