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Probing the structure and evolution of the Apo I and Co I proteins by single-molecule atomic force microscopy.
Numerous biochemical and biophysical studies have revealed that human apolipoprotein I (apo I) is closely associated with a variety of lipoproteins and functions to help the cells transport lipids and regulate the secretion of these proteins. It was proposed that the four glutamic acid residues at the C-terminal end of apo I, which are distinct from all known crystallographic or predicted apo I structures, form the lipid-binding region, accounting for the high affinity of apo I for lipoprotein particles. In the current study, we performed atomic force microscopy (AFM) measurements in contact mode on lipid-coated supported planar mica with both bovine apo I and recombinant human apo I. The results of AFM images revealed that both proteins retained the same globular structure as reported in crystallographic structures. Additionally, two interaction maps were constructed from the cross-correlation curves and the equilibrium dissociation constants (K(D)) of apo I-lipid complexes were determined. The average interaction K(D) of apo I with phosphatidylcholine (K(D) = 2.9 × 10(4) M(-1)) was approximately 10 times higher than that of apo I with phosphatidylcholine-cholesterol (K(D) = 5.8 × 10(3) M(-1)). Our results, together with recent structural data on apo I-containing lipoprotein particles from different mammals, indicated that the high affinity and specificity of apo I for the specific lipids in lipoproteins are well conserved during evolution.// Code generated by smithy-go-codegen DO NOT EDIT.

package types

import (
«github.com/aws/aws-sdk-go-v2/aws»
smithy «github.com/awslabs/smithy-go»
«github.com/awslabs/smithy-go/ptr

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