Human islet amyloid polypeptide at the air-aqueous interface: A Langmuir monolayer approach

Shanghao Li, Miodrag Micic, Jhony Orbulescu, Jeffrey D. Whyte, Roger Leblanc

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Human islet amyloid polypeptide (hIAPP) is the source of the major component of the amyloid deposits found in the islets of Langerhans of around 95 per cent type 2 diabetic patients. The formation of aggregates and mature fibrils is thought to be responsible for the dysfunction and death of the insulin-producing pancreatic β-cells. Investigation on the conformation, orientation and self-assembly of the hIAPP at time zero could be beneficial for our understanding of its stability and aggregation process. To obtain these insights, the hIAPP at time zero was studied at the air-aqueous interface using the Langmuir monolayer technique. The properties of the hIAPP Langmuir monolayer at the air-aqueous interface on a NaCl subphase with pH 2.0, 5.6 and 9.0 were examined by surface pressure- and potential-area isotherms, UV-Vis absorption, fluorescence spectroscopy and Brewster angle microscopy. The conformational and orientational changes of the hIAPP Langmuir monolayer under different surface pressures were characterized by p-polarized infrared-reflection absorption spectroscopy, and the results did not show any prominent changes of conformation or orientation. The predominant secondary structure of the hIAPP at the air-aqueous interface was α-helix conformation, with a parallel orientation to the interface during compression. These results showed that the hIAPP Langmuir monolayer at the air-aqueous interface was stable, and no aggregate or domain of the hIAPP at the air-aqueous interface was observed during the time of experiments.

Original languageEnglish
Pages (from-to)3118-3128
Number of pages11
JournalJournal of the Royal Society Interface
Volume9
Issue number76
DOIs
StatePublished - Nov 7 2012

Fingerprint

Islet Amyloid Polypeptide
Polypeptides
Monolayers
Air
Crystal orientation
Conformations
Pressure
Amyloid
Fluorescence Spectrometry
Amyloid Plaques
Fluorescence spectroscopy
Insulin
Absorption spectroscopy
Islets of Langerhans
Self assembly
Isotherms
Microscopy
Spectrum Analysis
Microscopic examination
Deposits

Keywords

  • hIAPP
  • Langmuir monolayer
  • Orientation
  • Protein
  • Stability

ASJC Scopus subject areas

  • Biophysics
  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Biomaterials
  • Biochemistry

Cite this

Human islet amyloid polypeptide at the air-aqueous interface : A Langmuir monolayer approach. / Li, Shanghao; Micic, Miodrag; Orbulescu, Jhony; Whyte, Jeffrey D.; Leblanc, Roger.

In: Journal of the Royal Society Interface, Vol. 9, No. 76, 07.11.2012, p. 3118-3128.

Research output: Contribution to journalArticle

Li, Shanghao ; Micic, Miodrag ; Orbulescu, Jhony ; Whyte, Jeffrey D. ; Leblanc, Roger. / Human islet amyloid polypeptide at the air-aqueous interface : A Langmuir monolayer approach. In: Journal of the Royal Society Interface. 2012 ; Vol. 9, No. 76. pp. 3118-3128.
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