Introduction In the last decades supramolecular chemistry has been intruduced as one of the most attractive fields in chemistry domain. This field has been defined as ‘, ‘, chemistry beyond the molecule’, ’,including systems based on molecular components that are held together by noncovalent intermolecular forces [1]. There are two Nobel Prize winners in this field firstly. Charles Pedersen, Donald J. Cram, and Jean-Marie Lehn’, s 1987 award for their development of crown ethers, carcerands, and cryptands, and secondary winners of the 2016 Nobel prizes Jean-Pierre Sauvage, Sir J. Fraser Stoddart, and Bernard L. Feringa for their introduction and advance of molecular machines [2]. Many applications have been reported for supramolecular chemistry...

Introduction Hydrogen bonding (HB) is a ubiquitous force in nature. It plays a crucial role in biocatalysis. Not until recently have chemists begun to implement this force in catalysis, but already with extraordinary success. However, chemists have only recently attempted to harness the power of using hydrogen bonds to perform catalysis, and the field is relatively undeveloped compared to research in Lewis acid catalysis. Nevertheless, the development of chiral Brø, nsted acids as activation forces is a highly challenging task in asymmetric catalysis, presumably because much weaker hydrogen-bonding interactions between the promoter and substrates would be the source of stereochemical control. Recently, chemists have begun to appreciate the potential offered by hydrogen bonding as a force for electrophile activation in smallmolecule-based catalysis. In particular, the utilization of chiral hydrogen-bond donors as promoters has been the subject of intense research, as evidenced by the number of research papers that have appeared....

Stereo-selectivity is an important feature in the development of the synthesis of biologically active organic compounds. In this process, (bio) catalysts exhibit substrate specificity that allows high levels of chemo- and regio-selectivity. Over the past decade, several peptides have been developed as effective bio-catalysts for a range of synthetically valuable reactions. In comparison with proteins owing a large number of amino acids and high molecular weights, peptide-catalysts possess only a few amino acid residues, which may adopt a secondary structure suitable for synthesis of desired chiral products. In addition, the flexible nature of peptides consents for tuning of reactivity and selectivity by replacing amino acid residues. These unique aspects provide attractive biocatalysts platform for asymmetric syntheses.