Dataset Information

HB digestion with Pepsin and Napsin

ABSTRACT: HB digestion with Pepsin and Napsin t=20, 60 and 120 min Analysis by nanoLC-ESI-iTRAP-OrbiTrap

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Dr. Sebastian Wiese

PROVIDER: MSV000087400 | MassIVE | Mon May 10 12:07:00 BST 2021

REPOSITORIES: MassIVE

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Publications

The C-terminal 32-mer fragment of hemoglobin alpha is an amyloidogenic peptide with antimicrobial properties.

Olari Lia-Raluca LR Bauer Richard R Gil Miró Marta M Vogel Verena V Cortez Rayas Laura L Groß Rüdiger R Gilg Andrea A Klevesath Raphael R Rodríguez Alfonso Armando A AA Kaygisiz Kübra K Rupp Ulrich U Pant Pradeep P Mieres-Pérez Joel J Steppe Lena L Schäffer Ramona R Rauch-Wirth Lena L Conzelmann Carina C Müller Janis A JA Zech Fabian F Gerbl Fabian F Bleher Jana J Preising Nico N Ständker Ludger L Wiese Sebastian S Thal Dietmar R DR Haupt Christian C Jonker Hendrik R A HRA Wagner Manfred M Sanchez-Garcia Elsa E Weil Tanja T Stenger Steffen S Fändrich Marcus M von Einem Jens J Read Clarissa C Walther Paul P Kirchhoff Frank F Spellerberg Barbara B Münch Jan J

Cellular and molecular life sciences : CMLS 20230517 6

Antimicrobial peptides (AMPs) are major components of the innate immune defense. Accumulating evidence suggests that the antibacterial activity of many AMPs is dependent on the formation of amyloid-like fibrils. To identify novel fibril forming AMPs, we generated a spleen-derived peptide library and screened it for the presence of amyloidogenic peptides. This approach led to the identification of a C-terminal 32-mer fragment of alpha-hemoglobin, termed HBA(111-142). The non-fibrillar peptide has ...[more]

PMID: 37198527

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Project description:Human ingestion of microplastics (MPs) is common and inevitable due to the widespread contamination of food items, but implications on the gastric digestion of food proteins are still unknown. In this study, the interaction between pepsin and polystyrene (PS) MPs was uncovered by investigating its effect on enzyme activity and conformation while in a simulated human gastric environment. The impact on food digestion was also determined by monitoring the kinetics of protein hydrolysis through static in vitro gastric digestion of cow’s milk contaminated with PS. The binding of pepsin to PS showed that surface chemistry of MPs dictates binding affinity. The key contributor to pepsin adsorption seems to be π−π interactions between the aromatic residues and the PS phenyl rings. During quick exposure (10 minutes) of pepsin to increasing concentrations (222, 2219, 22188 particles/mL) of 10 μm PS (PS10) and 100 μm PS (PS100), total enzymatic activities were not affected remarkably. However, upon prolonged exposure at 1 and 2 hours, preferential binding of pepsin to the small, low zeta-potential PS caused structural changes in the protein which led to a significant reduction of its activity. Digestion of cow’s milk mixed with PS10 resulted in transient accumulation of larger peptides (10-35 kDa) and reduced bioavailability of short peptides (2-9 kDa) in the gastric phase. This, however, was only observed at extremely high PS10 concentration (0.3 mg/mL or 5.46E+05 particles/mL). The digestion of milk peptides, bound preferentially over pepsin on the hard corona around PS10, was delayed up to 15 minutes in comparison to bulk protein digestion. Intact caseins, otherwise rapidly digested, remained bound to PS10 in hard corona for up to 15 minutes. This work presents valuable insights regarding the interaction of MPs, food proteins, and pepsin, and their dynamics during gastric digestion which provides new knowledge and understanding on the potential risks of MPs to human health.