Spontaneous transfer of monoacyl amphiphiles between lipid and protein surfaces. Academic Article uri icon

Overview

abstract

  • The kinetics of transfer of natural and fluorescent nonesterified fatty acids (NEFA) and lysolecithins (lysoPC) from phospholipid and protein surfaces were measured. The kinetics of transfer of 12-(1-pyrenyl)dodecanoic acid, from liquid crystalline and gel phase single unilamellar phospholipid vesicles, very low, low, and high density lipoproteins, human serum albumin, and rat liver fatty acid-binding protein, were first-order and characterized by similar rate constants. The halftimes (t1/2) of NEFA transfer from lipids and proteins were dependent on the acyl chain structure according to log t1/2 = -0.62n + 0.59m + 12.0, where n and m, respectively, are the numbers of carbon atoms and double bonds. The structure of the donor surface had a measurable but smaller effect on transfer rates. The kinetics of NEFA and lysoPC transfer are slow relative to the lipolytic processes that liberate them. Therefore, one would predict a transient accumulation of NEFA and lysoPC during lipolysis and an attendant modulation of many metabolic processes within living cells and within the plasma compartment of blood. These data will be useful in the refinement of current models of membrane and lipoprotein function and in the selection of fluorescent NEFA analogs for studying transport in living cells.

publication date

  • April 1, 1997

Research

keywords

  • Fatty Acids, Nonesterified
  • Lipid Metabolism
  • Lysophosphatidylcholines
  • Neoplasm Proteins
  • Nerve Tissue Proteins
  • Proteins
  • Surface-Active Agents

Identity

PubMed Central ID

  • PMC1184367

Scopus Document Identifier

  • 0030901275

Digital Object Identifier (DOI)

  • 10.1016/S0006-3495(97)78819-2

PubMed ID

  • 9083677

Additional Document Info

volume

  • 72

issue

  • 4