Barbara Biondi

1 Introduction Peptides are gaining increasing commercial interest in view of the growing number approved as drugs [1, 2]. Solid-phase peptide synthesis (SPPS), introduced in 1963 by Nobel laureate Bruce Merrifield [3], is currently the most exploited method for large-scale peptide production. SPPS is ea sily scalable, can be automated, and allows the synthesis of long peptides in short times. It significantly simplifies peptide synthesis as compared to classical solution methods.

Conflicts of Interest The authors declare no conflicts of interest. Data Availability Statement The data that supports the findings of this study are available in the supporting information of this article. Supporting Information Filename Description ejoc70793-sup-0001-SuppData-S1.pdf931.8 KB Characterization data of scaffolds A-C, scaffolds 1-3 and peptide Fmoc-Leu-Leu-Val-Phe-NH2 are available as supporting information.

1 Introduction Intramolecularly hydrogen-bonded turns, in which an N–H···O=C hydrogen bond takes place between nonconsecutive residues, are significant contributors to the 3D architecture of peptides and proteins [1]. In general, they might induce kinks, bends, and even reversal of the direction of the peptide backbone.