Structural Flexibility of Proteins Dramatically Alters Membrane Stability─A Novel Aspect of Lipid-Protein Interaction

Protein isoforms are structural variants with changes in the overall flexibility predominantly at the tertiary level. For membrane associated proteins, such structural flexibility or rigidity affects membrane stability by playing modulatory roles in lipid-protein interaction. Herein, we investigate...

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Bibliographic Details
Published in:The journal of physical chemistry letters 2022-12, Vol.13 (49), p.11430-11437
Main Authors: Giri, Rajendra P, Mukhopadhyay, Mrinmay K, Sanyal, Milan K, Bose, Dipayan, Chakrabarti, Abhijit, Quan, Peiyu, Bu, Wei, Lin, Binhua
Format: Article
Language:English
Subjects:
Chemistry
Materials Science
Membrane Proteins
Phospholipids - chemistry
Physics
Science & Technology - Other Topics
Spectrin - chemistry
Spectrin - metabolism
Spectrin - pharmacology
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Summary:Protein isoforms are structural variants with changes in the overall flexibility predominantly at the tertiary level. For membrane associated proteins, such structural flexibility or rigidity affects membrane stability by playing modulatory roles in lipid-protein interaction. Herein, we investigate the protein chain flexibility mediated changes in the mechanistic behavior of phospholipid model membranes in the presence of two well-known isoforms, erythroid (ER) and nonerythroid (NER) spectrin. We show dramatic alterations of membrane elasticity and stability induced by spectrin in the Langmuir monolayers of phosphatidylocholine (PC) and phosphatidylethanolamine (PE) by a combination of isobaric relaxation, surface pressure-area isotherm, X-ray scattering, and microscopy measurements. The NER spectrin drives all monolayers to possess an approximately equal stability, and that required 25-fold increase and 5-fold decrease of stability in PC and PE monolayers, respectively. The untilting transition of the PC membrane in the presence of NER spectrin observed in X-ray measurements can explain better membrane packing and stability.
ISSN:1948-7185
1948-7185
DOI:10.1021/acs.jpclett.2c02971