Conformational stability to pH changes of the NH2-terminal propeptide of human pulmonary surfactant protein B precursor

A. Bañares-Hidalgo; A. Palacios; A.G. Serrano; J. Pérez-Gil; P. Estrada

Conformational stability to pH changes of the NH₂-terminal propeptide of human pulmonary surfactant protein B precursor

In: Industrial, medical and environmental applications of microorganisms

Authors:

A. Bañares-Hidalgo

A. Bañares-Hidalgo Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain; estrada@bbm1.ucm.es

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A. Palacios

A. Palacios Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain; estrada@bbm1.ucm.es

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A.G. Serrano

A.G. Serrano Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain; estrada@bbm1.ucm.es

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J. Pérez-Gil

J. Pérez-Gil Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain; estrada@bbm1.ucm.es

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P. Estrada

P. Estrada Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain; estrada@bbm1.ucm.es

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Type:: Chapter

Pages:: 599–605

DOI:: https://doi.org/10.3920/9789086867950_108

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A recombinant form of the NH₂-terminal propeptide of human pulmonary surfactant protein B precursor (SP-B_N) has been produced in Escherichia coli. The conformational stability of the protein to pH acidification was studied by far-UV circular dichroism (CD). The secondary structure of the propeptide changed moderately from pH 7 to 4.1 and was much recovered after regaining neutrality. The emission of the fluorescent probe bis-ANS at pH 4.2 but not at neutral pH indicates that the propeptide adopts a molten globule-like state at pH 4. The effect of alkaline pH on the protein followed by CD and fluorescence spectroscopies indicates that the ionization of an amino acid residue with an apparent pK=8.05±0.15 was responsible of the observed conformational changes in the propeptide.

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Industrial, medical and environmental applications of microorganisms

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E-Book ISBN:: 9789086867950

Publisher:: Wageningen Academic

Print Publication Date:: 01 Nov 2014

Subjects
- Life Sciences

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Conformational stability to pH changes of the NH2-terminal propeptide of human pulmonary surfactant protein B precursor

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Industrial, medical and environmental applications of microorganisms

Current status and trends

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Conformational stability to pH changes of the NH₂-terminal propeptide of human pulmonary surfactant protein B precursor