The synthetic oligopeptide I undergoes a spontaneous, reversible transition from an α‐helix to a β‐sheet structure in mixtures of 45% 2,2,2‐trifluoroethanol and 55% H2O. The amphiphilic oligopeptide 1 and two isomers were expressly designed for this investigation. Such peptides, which can exist in several conformations, might find application as “switches” in the de novo design of artificial proteins. equation image

Eine plötzliche reversible Umwandlung α‐Helix → β‐Faltblatt beim synthetischen Oligopeptid 1 wurde in Mischungen aus 45% 2,2,2‐Trifluorethanol und 55% H2O beobachtet. Das amphiphile 1 und zwei Isomere wurden extra für diese Untersuchungen konstruiert. Solche in mehreren Konformationen auftretende Peptide könnten als „Schaltelemente”︁ beim de‐novo‐Design künstlicher Proteine Verwendung finden.

A report from a symposium on the prepn. and conformational properties of template-assembled synthetic proteins. [on SciFinder (R)]

The construction of a template‐assembled synthetic protein (TASP) designed to contain both a 4‐helix bundle and a β‐barrel as two folding “domains” is described. For the de novo design of proteins, amphiphilic helices (α) and β‐sheets (β) are covalently attached to a template peptide (T) carrying functional side chains suitably oriented to promote intarmolecular folding of the secondary structure blocks into a characteristic packing arrangement, i.e., T8‐(4α)(4β). The design of this new macromolecule was assisted by computer modeling, which suggested a low‐energy conformation with tight hydrophobic packing of the secondary structure subunits. Solid‐phase synthesis of the “two‐domain” TASP molecule was achieved using orthogonal protection techniques. The solution properties as well as circular dichroism (CD) and infrared spectroscopy (IR) data under various experimental conditions are consistent with the folded conformation suggested by modeling.

ChemInformVolume 20, Issue 34 Natural Products ChemInform Abstract: Efficient Synthesis of N-Triphenylmethyl-α-amino Acids. M. MUTTER, M. MUTTER Inst. Org. Chem., FU, Fachb. Chem., D-1000 Berlin 33Search for more papers by this authorR. HERSPERGER, R. HERSPERGER Inst. Org. Chem., FU, Fachb. Chem., D-1000 Berlin 33Search for more papers by this author M. MUTTER, M. MUTTER Inst. Org. Chem., FU, Fachb. Chem., D-1000 Berlin 33Search for more papers by this authorR. HERSPERGER, R. HERSPERGER Inst. Org. Chem., FU, Fachb. Chem., D-1000 Berlin 33Search for more papers by this author First published: August 22, 1989 https://doi.org/10.1002/chin.198934322Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume20, Issue34August 22, 1989 RelatedInformation

A new one-pot synthesis of N-triphenylmethyl(trityl) α-amino acids 3 via their trityl ester 2 has been developed.

AbstractA new general strategy for the construction of artificial proteins with predetermined tertiary structure is presented. Amphiphilic α‐helix and β‐sheet‐forming oligopeptides are assembled on a multifunctional ttemplate molecule which directs the peptide blocks to adopt characteristic folding topologies. The design, synthesis, and conformational properties of these template‐assembled synthetic proteins (TASP) are exemplified for βαβ‐, α‐helix‐bundle‐ and β‐barrel‐like tertiary structures using specially designed oligopeptides as template molecules. In contrast to linear polypeptide chains of comparable molecular weights, these conceptually novel marcromolecules are readily accessible to chemical synthesis and exhibit excellent solubility in a number of solvents. Experimental evidence is provided for a template‐induced intramolecular folding to secondary and tertiary structures in aqueous solutions. This approach opens new prospects for the chemical construction of biomacromolecules with tailormade structural and functional properties.