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10.1021/acs.biochem.6b01132 http://scihub22266oqcxt.onion/10.1021/acs.biochem.6b01132 C5359774!5359774!28029249     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28029249&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Biochemistry 2017 ; 56 (3): 445-57 Nephropedia Template TP {{tp|p=28029249|t=2017. Structure and Function of AApeptides |pdf=|usr=}}{{28029249}} gab.com Text Structure and Function of AApeptides JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=28029249 #FOAvip The intrinsic drawbacks encountered in bioactive peptides in chemical biology and biomedical sciences have diverted research efforts to the development of sequence-specific peptidomimetics that are capable of mimicking the structure and function of peptides and proteins. Modifications in the backbone and/or the side chain of peptides have been explored to develop biomimetic molecular probes or drug leads for biologically important targets. To expand the family of oligomeric peptidomimetics to facilitate their further application, we recently developed a new class of peptidomimetics, AApeptides based on a chiral peptide nucleic acid backbone. AApeptides are resistant to proteolytic degradation and amenable to enormous chemical diversification. Moreover, they could mimic the primary structure of peptides and also fold into discrete secondary structure such as helices and turn-like structures. Furthermore, they have started to show promise in applications in material and biomedical sciences. Herein, we highlight the structural design and some function of AApeptides and present our perspective on their future development. Twit Text FOAVip Structure and Function of AApeptides ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=28029249 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28029249 #FOAvip English Wikipedia <ref>{{Cite pmid|28029249}}</ref> Structure and Function of AApeptides #MMPMID28029249 Bolarinwa O; Nimmagadda A; Su M; Cai J Biochemistry 2017[Jan]; 56 (3): 445-57 PMID28029249show ga The intrinsic drawbacks encountered in bioactive peptides in chemical biology and biomedical sciences have diverted research efforts to the development of sequence-specific peptidomimetics that are capable of mimicking the structure and function of peptides and proteins. Modifications in the backbone and/or the side chain of peptides have been explored to develop biomimetic molecular probes or drug leads for biologically important targets. To expand the family of oligomeric peptidomimetics to facilitate their further application, we recently developed a new class of peptidomimetics, AApeptides based on a chiral peptide nucleic acid backbone. AApeptides are resistant to proteolytic degradation and amenable to enormous chemical diversification. Moreover, they could mimic the primary structure of peptides and also fold into discrete secondary structure such as helices and turn-like structures. Furthermore, they have started to show promise in applications in material and biomedical sciences. Herein, we highlight the structural design and some function of AApeptides and present our perspective on their future development. äStructure and Function of AApeptides (epmc).pdf DeepDyve Pubget Overpricing