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One of the most desirable properties that biomaterials designed for tissue engineering or drug delivery applications should fulfill is biodegradation and resorption without toxicity. Therefore, there is an increasing interest in the development of biomaterials able to be enzymatically degraded once implanted at the injury site or once delivered to the target organ. In this paper, we demonstrate the protease sensitivity of self-assembling amphiphilic peptides, in particular, RAD16-I (AcN-RADARADARADARADA-CONH2), which contains four potential cleavage sites for trypsin. We detected that when subjected to thermal denaturation, the peptide secondary structure suffers a transition from β-sheet to random coil. We also used Matrix-Assisted Laser Desorption/Ionization-Time-Of-Flight (MALDI-TOF) to detect the proteolytic breakdown products of samples subjected to incubation with trypsin as well as atomic force microscopy (AFM) to visualize the effect of the degradation on the nanofiber scaffold. Interestingly, thermally treated samples had a higher extent of degradation than non-denatured samples, suggesting that the transition from β-sheet to random coil leaves the cleavage sites accessible and susceptible to protease degradation. These results indicate that the self-assembling peptide can be reduced to short peptide sequences and, subsequently, degraded to single amino acids, constituting a group of naturally biodegradable materials optimal for their application in tissue engineering and regenerative medicine. [ABSTRACT FROM AUTHOR]

Milk proteins are recognized as the main source of biologically active peptides. Casein's primary structure contains several bioactive amino acid sequences on its latent inactive form. These potential active sequences can be released during cheese manufacture and ripening, giving rise to peptides with biological activity such as antihypertensive, antidiabetic, antioxidant, immunomodulatory, and mineral‐binding properties. However, the presence of biopeptides in cheese does not imply actual biological activity in vivo because these peptides can be further hydrolyzed during gastrointestinal transit. This paper reviews the recent advances in biopeptide formation in ripened cheeses production, focusing on the influence of technological parameters affecting proteolysis and the consequent release of peptides. The main discoveries in the field of cheese peptide digestion through recent in vivo and in vitro model studies are also reviewed. © 2021 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Many useful properties are assigned to camel ( Camelus dromedarius ) milk, which is traditionally used for the treatment of tuberculosis, gastroenteritis, and allergy in many countries. Some amino acid sequences, which are encrypted in the camel proteins, may play a beneficial role in human health once they are released from milk either in vivo during normal digestion or by proteolysis with purified enzymes or during bacterial fermentation. Similar to the bovine milk counterparts, camel milk bioactive peptides may display a variety of potential activities that were almost always unveiled from in vitro analyses: anti-microbial, anti-oxidative, anti-hypertensive, anti-inflammatory, and immunomodulatory activities. Today, there is a growing interest for bioactive peptides generated from camel milk. This paper reviews available data on the potential biological activities of the camel milk proteins and their peptides liberated either during milk fermentation with proteolytic bacterial strains or by enzyme hydrolysis with specific proteases or simulated gastro-intestinal digestion. [ABSTRACT FROM AUTHOR]