Peptides/polypeptides peptoids

Like peptide oligomers, peptoids can be analyzed by HPLC and by mass spectrometry. They can be sequenced by Fdman degradation [13] or by tandem mass spectrometry [14] since, like polypeptides, they conveniently fragment along the main chain amides [15, 16]. 

Polypeptoids are similar to polypeptides except the side chains are attached to the amide nitrogen of the peptide backbone instead of the a -carbon (Figure 12.6). Peptoids are synthesized by solid-phase synthesis on a peptide synthesizer using a submonomer approach that proceeds by adding each monomer in a two-step process. With this method, many different side chain groups... 

FSCE can also show impurities present in solid-phase synthesis products that are not clearly evident by conventional purification methods. RP-HPLC with ultra violet (UV) detection is traditionally used to analyze solid-phase synthesis products such as peptoids and peptides as well as to separate them preparatively away from any deletion products. Since each synthetic monomer addition cycle is less than 100% efficientj products that are one or two monomer units shorter than the desired product must be purified out to ensure monodispersity of the final polypeptide or polypeptoid. The separating power of FSCE was compared with analytical RP-HPLC traces after RP-HPLC purification (Figure 12.7). The one peak in the RP-HPLC trace actually separates into one large peak... 

Abstract Life as we know it is impossible without formation of hierarchical structures. First and foremost, proteins, that is, sequence-specific polypeptides, are nature s vanguard in this respect. Peptoids and polypeptoids are structural isomers and analogs to peptides and polypeptides. Here, we review the advancements over the last few years on biomimetic hierarchical stmctures obtained using polypeptoids. Although the inherently more flexible amide bond in peptoids make the stabilization of secondary stmcture challenging, it also gives us a tool to direct the conformation of the amide bond by design. As will be seen, this is a particularly important feature of peptoids. 

Peptoids have been used as model compounds for many decades to better understand the behavior of peptides. Recently, Zuckermann et al. designed a peptoid 100-mer to study the coil-to-globule transition [93]. It has been established that hydrophobic interactions are an important driving force in the folding of polypeptides in proteins [94—98]. 

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