This issue of Peptide Science is a testimonial to brilliance packaged in a nontraditional way. We are honoring the contributions of Louis A. Carpino (“Lou” to many of us or “Louie” to a few), who passed away in January 2019 at the age of 91. Lou Carpino's contributions to peptide chemistry specifically, and organic chemistry more broadly, over the course of his career are truly stunning as summarized

Unfortunately, over the last 12 months, the peptide science community has lost several colleagues, notably, Judy Warner, American Peptide Society (APS) Symposium organizer, Elizabeth Schram, the American Peptide Symposium Young Investigator sponsor, and Professor Jean Rivier, the president of the APS (1993‐1995). Judy was a wonderful person, always gentle and cheerful, and dedicated to the organization

Cover caption: The aggregation behaviour of peptide fragments of proteins in aqueous solutions with ionic liquids (ILs) could help identify the relationship between IL–protein interactions and structural behaviour of intrinsically disordered proteins in this media. Takekiyo et al. report that the addition of 1‐butyl‐3‐methylimidazolium thiocyanate, but not ethylammonium nitrate, to amyloid β1–11 peptide

The 8th Peptide Engineering Meeting took place in Berlin, Germany, in November 2018. The reviews and original articles collated in this issue present an extract of the talks, poster presentations and scientific discussions of the conference as an attempt to showcase the current state‐of‐the‐art in the field of peptide, protein and carbohydrate engineering.

Protein secondary and tertiary structure mimics have served as model systems to probe biophysical parameters that guide protein folding and as attractive reagents to modulate protein interactions. Here, we review contemporary methods to reproduce loop, helix, sheet, and coiled‐coil conformations in short peptides.

Pauling and Corey proposed in 1953 that equimolar mixtures of all‐L and all‐D peptides may form two‐dimensional arrays with alternating chirality sense, termed rippled β‐sheets, in contrast with pleated β‐sheets formed by enantiopure (all‐L OR all‐D) peptides. Numerous enantiopure Aβ structures have been reported, providing beautiful examples of pleated cross‐β structures. Although indirect evidence

Accomplishment of efficient intracellular delivery of bioactive peptides and proteins have been reported via conjugation of peptides having membrane permeation ability (i.e., cell‐penetrating peptides [CPPs]), where a physiological uptake system of extracellular materials, endocytosis, often plays a role. When endocytosed, the bioactive peptides and proteins are encapsulated into vesicular compartment

The primary structure of collagen, the major protein in connective tissue of mammals, comprises of repeating triads [(LPro‐LHyp‐Gly)n, P1, LHyp being 4R‐hydroxy‐lProline)] in a single strand that adopts left‐handed polyproline II type helix. Three such single stranded helices wind around each another and held together by interchain H‐bonds to form right‐handed triple helix. This manuscript reports

Understanding the aggregation selectivity of peptide fragments of full‐length proteins in aqueous solutions with ionic liquids (ILs) could facilitate the elucidation of the relationship between the IL‐protein interactions and structural behavior of intrinsically disordered proteins (IDPs) such as amyloid β protein following the addition of ILs. In the present study, we investigate structural changes

Racemic mixtures frequently display properties that are different from those associated with their enantiopure counterparts, and are often characterized by higher propensity to form aggregates. Our previous research established that mixing of the enantiomers of Alzheimer amyloid β (Aβ) 42 peptides is an effective strategy to induce an oligomer‐to‐fibril conversion, which puts Aβ42 into a substantially