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High concentration solubility and stability of ɛ-poly-l-lysine in an ammonium-based ionic liquid: A suitable media for polypeptide packaging and biomaterial preparation

Author:
Sequeira, Rosy Alphons, Singh, Nripat, Pereira, Matheus M., Chudasama, Nishith A., Bhattacharya, Sourish, Sharma, Mukesh, Mondal, Dibyendu, Prasad, Kamalesh
Source:
International journal of biological macromolecules 2018 v.120 pp. 378-384
ISSN:
0141-8130
Subject:
DNA, Streptomyces albulus, ammonium, ammonium acetate, anions, biobased products, choline, computer simulation, formates, gels, ionic liquids, polypeptides, proteins, solubility
Abstract:
Packaging of structurally sensitive biomolecules such as proteins, peptides and DNA in non-aqueous media at ambient conditions with chemical and structural stability is important to explore the potential of such biomacromolecules as substrate for functional biomaterial design and for biotechnological applications. In this perspective, solubility, chemical and structural stability of ɛ-poly-l-lysine (ɛ-PL), a homopolypeptide produced by Streptomyces albulus in different ionic liquids (ILs) namely 2-hydroxyethyl ammonium formate (2-HEAF), 2-hydroxyethyl ammonium acetate (2-HEAA), choline formate (Ch-Formate) and choline acetate (Ch-Acetate) was studied. Maximum solubility (15% w/v) of the homopolypeptide was observed in 2-HEAF and lowest was found in Ch-Formate (2% w/v). After regeneration of the dissolved polypeptide in the IL, the IL could be recycled and reused in the dissolution process. Unlike in other ILs, 3–15% w/v of ɛ-PL in 2-HEAF gave formation of a thixotropic thermoreversible soft gel. Molecular docking studies established favourable interactions of [2-HEA]+ cation over [Ch]+ with ɛ-PL indicating [2-HEA]+ as the most promising cation for the dissolution process. However, the role of the anions was also found to be important, which could lead to improvement in polypeptide solubility when combined to the selected cation. The findings demonstrate suitability of the ionic liquids for functionalization of polypeptides for biomaterial preparation.
Agid:
6154476