Peptide derived C. striata albumin as a natural angiotensin-converting enzyme inhibitor

Guntur Berlian; Catur Riani; Neng Fisheri Kurniati; Heni Rachmawati

doi:10.1016/j.heliyon.2023.e15958

Peptide derived C. striata albumin as a natural angiotensin-converting enzyme inhibitor

Heliyon. 2023 Apr 29;9(5):e15958. doi: 10.1016/j.heliyon.2023.e15958. eCollection 2023 May.

Authors

Guntur Berlian^{1

2}, Catur Riani¹, Neng Fisheri Kurniati³, Heni Rachmawati^{1

4}

Affiliations

¹ Department of Pharmaceutics, School of Pharmacy, Bandung Institute of Technology, Ganesha 10, Bandung 40132, Indonesia.
² Mega Medica Pharmaceuticals, Kalideres, Jakarta Barat 11840, Indonesia.
³ Department of Pharmacology-Clinical Pharmacy, School of Pharmacy, Bandung Institute of Technology, Ganesha 10, Bandung 40132, Indonesia.
⁴ Research Center for Nanosciences and Nanotechnology, Bandung Institute of Technology, Ganesha 10, Bandung 40132, Indonesia.

Abstract

As one of the most popular sources for fish albumin, Channa striata has been considered as a promising substitute for human albumin. However, scientific information regarding its genomic and proteomic is very limited, making its identification rather complicated. In this study, we aimed to isolate, characterize, and examine the bioactivity of protein and peptide derivatives of C. striata albumin. Fractionation of albumin from C. striata extract was conducted using Cohn Process and the yield was evaluated. The peptides were further produced by enzymatic hydrolysis. All these proteins were studied using tricine-SDS PAGE and tested for in vitro ACE inhibition. Dry weights of the Fraction-5, where the albumin was more abundant and purer, was 3.8 ± 2.1%. Based on tricine-SDS PAGE analysis, two bands of protein, e.g., approximately 10 and 13 kDa, were detected with highest intensity found in Fraction-5, which might be albumin of C. striata. An increasing trend of ACE inhibition by the fractions was observed, ranging from 7.09 to 22.99%. The highest ACEI activity was found in peptides from alcalase hydrolysis with molecular size <3 kDa (56.65 ± 2.32%, IC₅₀ 36.93 μg/mL). This value was also statistically significant compared with the non-hydrolyzed Fraction-5 and Parental Fraction, which were 23.48 ± 3.11% (P < 0.05) and 13.02 ± 0.68% (P < 0.01), respectively. Taken together, these findings suggest a promising potential of peptide-derived C. striata albumin for natural antihypertensive agents.

Keywords: ACEI; Albumin; Anti-hypertension; Bioactive peptide; Channa striata; Cohn process.