Surfactant protein B: lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain.
نویسندگان
چکیده
The mechanisms by which pulmonary surfactant protein B (SP-B) affects the surface activity of surfactant lipids are unclear. We have studied the peptide/lipid interactions of the amino-terminal amphipathic domain of SP-B by comparing the secondary conformations and surface activities of a family of synthetic peptides based on the native human SP-B sequence, modified by site-specific amino acid substitutions. Circular dichroism measurements show an alpha-helical structure correlating with the ability of the peptides to interact with lipids and with the surface activity of peptide/lipid dispersions. Amino acid substitutions altering either the charge or the hydrophobicity of the residues lowered the helical content and reduced the association of the aminoterminal segment with lipid dispersions. Surface activity of peptide/lipid mixtures was maximally altered by reversal of charge in synthetic peptides. These observations indicate that electrostatic interactions and hydrophobicity are important factors in determining optimal structure and function of surfactant peptides in lipid dispersions.
منابع مشابه
Structural features of synthetic peptides of apolipoprotein E that bind the LDL receptor.
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متن کامل1674 ApoB - 100 Has a Pentapartite Structure Composed of Three Amphipathic ar - Helical Domains Alternating With Two Amphipathic / 3 - Strand Domains Detection by the Computer Program
Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...
متن کاملApoB - 100 Has a Pentapartite Structure Composed of Three Amphipathic ar - Helical Domains Alternating With Two Amphipathic / 3 - Strand Domains Detection by the Computer Program
Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...
متن کاملApoB-100 Has a Pentapartite Structure Composed of Three Amphipathic ar-Helical Domains Alternating With Two Amphipathic /3-Strand Domains
Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...
متن کامل1674 ApoB - 100 Has a Pentapartite Structure Composed of Three Amphipathic ar - Helical Domains Alternating With Two Amphipathic / 3 - Strand Domains
Due to the great length of apolipoprotein (apo) B-100, the localization of lipid-associating domains in this protein has been difficult. To address this question, we developed a computer program called LOCATE that searches amino acid sequences to identify potential amphipathic a-helixes and /3-strands by using sets of rules for helix and strand termination. A series of model chimeric protein te...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 88 16 شماره
صفحات -
تاریخ انتشار 1991