상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B

Authors 

Joo Hyun KangMyung Kyu LeeKil Lyong KimKyung Soo Hahm

Publisher 

International Union of Biochemistry and Molecular Biology

Issue Date 

1996

Citation 

Biochemistry and Molecular Biology International, vol. 40, no. 3, pp. 617-627

Keywords 

lung surfactantproteinsynthetic peptideprotein secondary structurepeptide fragmentsphospholipidsprotein structuresecondarypulmonary surfactantsstructure-activity relationship

Abstract 

Synthetic pulmonary surfactants consisting of a mixture of phospholipids with synthetic peptides based on human and bovine surfactant-associated protein SP-B were prepared. These surfactants were analyzed for their biophysical activities by Wilhemly balance experiments and for their secondary structures by circular dichroism (CD) spectroscopy. Four synthetic peptides (SP-1, SP-2, SP-3, and SP-4) combined with the phospholipid mixture displayed significant surfactant properties. The CD spectra showed that the α-helical propensities of the peptides in SDS micelles were related to their surfactant activities. These results suggested that the several truncated peptides originated from SP-B protein, when appropriately recombined with phospholipids, could be used as an effective synthetic surfactant for clinical use.

ISSN 

1039-9712

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)