As is known, peptides have played a crucial role in fundamentally physiological and biochemical functions of life. For decades now, peptides research is a continuously growing field of science. With the rapid development of modern biotechnology, an increasing number of special design platforms for the design and screening of peptides have attracted public concerns. However, people hold different opinions about such issue.
Since the design platform is important, it has played its full role in recent years. Taking synthetic peptides as an example, such peptides may be useful in structure-function studies of polypeptides, as peptide hormones and hormone analogues, in the preparation of cross-reacting antibodies, and in the design of novel anti-microbial and anti-cancer drugs. The main reasons that they are widely used are as followed: to verify the structure of naturally existed peptides as determined by degradation techniques and study the close relationship between structure and activity of biologically active peptides. In addition, in order to develop new peptide-based immunogens, hormones, vaccines and some other substances, a high-throughput design platform for the practical functions of peptides is absolutely necessary.
In fact, there are many naturally-occurring peptides that are biologically active. If a patient does not naturally produce a peptide that he needs, this peptide can be synthesized as well. While on the other hand, the process of design and screening might be sort of complex, in terms of the applicant realms of various peptides. In addition, the amino acids in an active peptide can be altered to make analogues of the original peptide. Taking the design and screening of short peptides as the instance, which is connected with the inhibitors of calcium oxalate monohydrate crystals, the two approaches should be arranged in varying sequences that mimic ubiquitous motifs in natural calcium-binding proteins. More specifically, they are screened utilizing a quick assay, for the purpose of measuring their efficiency for inhibiting COM crystallization.
Briefly speaking, the results of design and screening of peptides might show that subtle variations in the placement of Ala and Asp residues in the peptide sequence can have a profound effect on the inhibition potential. Therefore, establishing new paradigms for the design and screening of peptides is extremely necessary.