Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Abstract

The effect of enzymatic hydrolysis by Savinase on the interfacial properties and antihypertensive activity of shrimp waste proteins was evaluated. The physicochemical characterization, interfacial tension, and surface characteristics of shrimp waste protein hydrolysates (SWPH) using different enzyme/substrate (E/S) (SWPH5 (SWPH using E/S = 5), SWPH15 (SWPH using E/S = 15), and SWPH40 (SWPH using E/S = 40)) were also studied. SWPH5, SWPH15, and SWPH40 had an isoelectric pH around 2.07, 2.17, and 2.54 respectively. SWPH5 exhibited the lowest interfacial tension (68.96 mN/m) followed by SWPH15 (69.36 mN/m) and SWPH40 (70.29 mN/m). The in vitro ACE inhibitory activity of shrimp waste protein hydrolysates showed that the most active hydrolysate was obtained using an enzyme/substrate of 15 U/mg (SWPH15). SWPH15 had a lower IC50 value (2.17 mg/mL) than that of SWPH5 and SWPH40 (3.65 and 5.7 mg/mL, respectively). This hydrolysate was then purified and characterized. Fraction F1 separated by Sephadex G25 column which presents the best ACE inhibition activity was then separated by reversed‐phase high performance liquid chromatography. Four ACE inhibitory peptides were identified and their molecular masses and amino acid sequences were determined using ESI–MS and ESI–MS/MS, respectively. The structures of the most potent peptides were SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR. The structural modeling of anti‐ACE peptides from shrimp waste through docking simulations results showed that these peptides bound to ACE with high affinity.

In Vitro Bioactivity of Astaxanthin and Peptides from Hydrolisates of Shrimp (Parapenaeus longirostris) By-Products: From the Extraction Process to Biological Effect Evaluation, as Pilot Actions for the Strategy “From Waste to Profit”

“…Figure 4 shows that lower-molecular-weight Pep have higher IA than PH, in accordance with Krichen et al’s results [ 48 ], which indicated a higher activity in peptide fractions from protein hydrolysates of shrimp waste ( P. longirostris ) than in whole hydrolysates.…”

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

“…This diversity, together with the availability of marine resources, have driven the search for new antihypertensive agents, which could be administered as functional foods or dietary supplements. Since the first discovery of a marine-derived peptide with ACE-inhibitory activity, researchers have identified a variety of antihypertensive peptides in hydrolysates from marine species, such as Synodus macrops [ 12 ] (AGPPGSDGQPGAK, IC 50 = 0.42 mM), Salmo salar [ 13 ] (GAR and IGPR, IC 50 = 0.598, 0.43 mM), shrimps (SSSKAKKMP, IC 50 = 0.88 mM) [ 14 ], and Ruditapes philippinarum (pRPH, tRPH and nRPH, IC 50 = 0.42, 2.93 and 3.53 mg/mL) [ 15 ]. Some marine-derived peptides are currently being evaluated for safety and efficacy through ongoing clinical trials which have advanced to different phases, and even a small number have entered the market.…”

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides From Fermented Bovine Milk Started by Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105: Purification, Identification, and Interaction Mechanisms

“…Additionally the sequence of these four ACE-inhibitory peptides are Lys-Pro-Ala-Gly-Asp-Phe (Z-I-1), Lys-Ala-Ala-Leu-Ser-Gly-Met (Z-I-2), Lys-Lys-Ala-Ala-Met-Ala-Met (Z-I-3), and Leu-Asp-His-Val-Pro-Gly-Gly-Ala-Arg (Z-I-4). Krichen et al (2018) reported the extraction of four ACE-inhibitory peptides from shrimp and showed that hydrophobic amino acids at the N-terminus might contribute to an increase in the ACE-inhibitory activity of peptides. Here, Leu-Asp-His-Val-Pro-Gly-Gly-Ala-Arg similarly has leucine at the N-terminal end.…”

“…ACE plays a critical role in these pathways to maintain blood pressure at a balanced level (Rice et al, 2004; Sanli et al, 2018). The inhibitory activities of ACE are considered to be an effective way to treat hypertension (Krichen et al, 2018). Many synthetic ACE inhibitors, which are used to regulate blood pressure during clinical treatment, present some safety hazards for humans, such as potential induced coughing, renal impairment, and allergic reactions (Alhaj, 2017).…”