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Hydrophobic Interaction Between Domain I of Albumin and B Chain of Detemir May Support Myristate-Dependent Detemir-Albumin Binding

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An Erratum to this article was published on 02 December 2016

Abstract

The bindings of detemir [LysB29(Nε-tetradecanoyl)des(B30)-insulin] with two highly homologous albumins, HSA (human serum albumin) and BSA (bovine serum albumin), were investigated through CD, spectrofluorophotometry, and molecular docking analysis. The absence of any tryptophanyl residue in detemir makes albumin binding study possible by exclusive tryptophanyl spectral quenching at 340 nm (λem = 296 nm). The interactions found to be static (Kq > 1010 M−1 s−1) with Stern–Volmer constants ≈103 M−1. The observed ΔG 0 that was negative in all cases concludes the reactions were spontaneous. Domains I and III of an albumin unfold with 5.0 M urea at pH 7.4, although domain II remains intact. Significant decreases in ΔH 0 and ΔS 0 were due to unfolding explicit that detemir binding may involve domains I and III of albumins. Temperature-dependent changes in binding were higher in HSA than BSA but after unfolding such changes were very less, further indicating the role of domains I and III in detemir binding. Pro28 and Tyr26 of insulin were found to be interacting with Arg114 and Val116 of HSA domain I, while myristate segment of detemir binds to Lys519 of domain III. Interactions seem to be predominantly hydrophobic and entropy driven. Although detemir binds to albumin through myristate, the peptide part shows involvement in binding.

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Abbreviations

HSA:

Human serum albumin

BSA:

Bovine serum albumin

Ksv:

Stern–Volmer constant

Kq:

Quenching constant

K :

Binding constant

n :

Number of binding sites

ΔG 0 :

Standard free energy change

ΔH 0 :

Standard change in enthalpy

ΔS 0 :

Standard change in entropy

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Authors and Affiliations

  1. Genes and Proteins Lab, Department of Biotechnology, Jamia Millia Islamia, New Delhi, 110025, India

    Sadaf Fatima

  2. Centre for Bioseparation Technology, VIT University, Vellore, 632014, India

    Priyankar Sen

  3. Department of Integrative Biology, School of Bio Sciences and Technology, VIT University, Vellore, 632014, India

    P. Sneha & C. George Priyadoss

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  1. Sadaf Fatima
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  2. Priyankar Sen
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  4. C. George Priyadoss
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Correspondence to Sadaf Fatima.

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The original version of this article was revised: There's an error in one of the author's name. C. George Priyadoss was incorrectly captured as C. George Priya Doss.

An erratum to this article is available at http://dx.doi.org/10.1007/s12010-016-2351-x.

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Fatima, S., Sen, P., Sneha, P. et al. Hydrophobic Interaction Between Domain I of Albumin and B Chain of Detemir May Support Myristate-Dependent Detemir-Albumin Binding. Appl Biochem Biotechnol 182, 82–96 (2017). https://doi.org/10.1007/s12010-016-2312-4

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