Pharmaceutical industry presenter protein properties

As evident from the previous discussion, a major barrier to the use of peptides as clinically useful drugs has to do with their poor delivery properties, because proteolytic enzymes present at most routes of administration are able to quickly metabolize most peptides. Peptides and proteins are, for the most part, hydrophilic in nature and, for this reason, do not readily penetrate lipophilic biomembranes. As well, they have short biological half-lives because of rapid metabolism and clearance, all of which deters from their efficient use in drug therapy. It is for these reasons that alternative drug delivery methods for peptides and proteins are an area of particular interest to the pharmaceutical industry. 

These natural compounds are of particular relevance due to their biological activities that contribute to the therapeutic properties attributed to some plants, especially those highlighted since many years ago by the traditional Chinese medicine. These features make flavanols a particular target of the pharmaceutical industry. Besides this, flavanols are also responsible for some antioxidant and sensorial properties presented in fruits and fruit-derived products. The astringency sensation is one of those properties resulting from the interaction between flavanols and salivary proteins in the oral cavity. On the other hand, flavanols can also... 

Transaminases are most powerful tools for the synthesis of chiral amines, amino acids, and amino alcohols, hi this chapter several approaches for tiie preparation of fine chemicals or building blocks for pharmaceuticals were discussed, like asymmetric synthesis or kinetic resolution. The main limitations of transaminase-catalyzed reactions are the need to shift the equihbrium to the product side and substrate and product inhibition. Some solutions to overcome such inhibition were presented here for example, multienzyme cascades or biphasic extraction of the product. Protein engineering by directed evolution or rational enzyme design is a promising option to find transaminases with different substrate specificities and enantiopreferences. This is becoming more and more important for the pharmaceutical industry. Furthermore, it is a way to alter enzyme properties known so far, like thermostability and solvent and pH stability. Protein engineering has been assisted by the recently solved structures of certain transaminases. 

Contrary to other whey proteins, a Fe " ion is present in lactoferrin molecule [3]. Similarly to immunoglobulins, it has the antimicrobial character [46]. Whey is appropriate for extraction of lactoferrin and cation-exchange chromatography is proposed for its purihcation. Heat treatment at pH 4.0 does not denature the protein therefore, this pH is suitable for its pasteurization. Recently, some beneficial aspects of lactoferrin on human s health have been regarded. Its exceptional properties such as antiinfective, anticancer, antioxidant and antimicrobial activities enhance its utility in pharmaceutical and food industries. Remarkably, lower pH values (2-3) enhance its antibacterial activity. The results of clinical studies about positive effects of lactoferrin on human and animals health have been published [49]. 

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