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A single amino acid in a peptide sequence can play an important role to tune the self‐assembly and hydrogelation behaviour. Here, a C‐terminal cysteine‐containing ultrashort peptide hydrogelator forms hydrogel through non‐covalent and covalent interactions. Interestingly, the hydrogel is insoluble in water and buffer solutions at different pH values (1‐13) and is thixotropic and injectable. In recent years, removing dyes from contaminated water has become a significant concern because of the shortage of freshwater resources. Therefore, the adsorption of dyes through a reliable, straightforward, nontoxic, cheap, and environmentally friendly adsorbent has become a popular topic. Hence, the hydrogelator was exploited to remove organic dyes from wastewater, harnessing its applicability in the gel phase and solid supports (filter paper and cotton). [ABSTRACT FROM AUTHOR]

The alteration of amino acid register in peptides could affect their folding properties and thus functions. The effect of sequence in metal ion induced folding of peptide/protein is important in the design of new functional protein structures, such as biomimetics. In this paper, a set of hairpin peptides with identical composition but different histidine locations have been designed to exploit the metal ion‐mediated peptide intramolecular folding transformation through the adjustment of histidine and lysine residue locations. The results demonstrated that the histidine positions in peptide sequence could dramatically affect the coordination modes between peptides and Cu(II) ion. The Cu(II) coordination could affect the secondary structure transformation and self‐assembly along with electrostatic interaction and hydrogen bonding synergistically. Three molecules with VHVH sequence at each side of the turn segment (VDPPT) were apt to coordinate with Cu(II) ion with three or four histidines. The closer the VHVH motifs were to the turn segment, the more easier the molecules were to form β sheet structure with the promotion of Cu(II) ions. These results demonstrated that the purposeful location of key amino acids in peptides could achieve the controllable conformation transformation of hairpin peptides, which provides useful strategies for biomimetic design, such as metalloenzymes. [ABSTRACT FROM AUTHOR]

A histidine‐containing bola‐amphiphilic molecule (NDIP) containing a peptide‐appended naphthalenediimide (NDI) forms fluorescent hydrogels in phosphate buffer and organogels with benzenoid solvents. These gels were characterized by several spectroscopic and microscopic techniques including FT‐IR, HR‐TEM, powder X‐ray diffraction and small‐angle X‐ray scattering, UV‐Vis and fluorescence studies. The gelator molecule exhibits no significant fluorescence in the xerogel state, while it shows a significant fluorescence (bright cyan) in the presence of volatile organic/inorganic acid vapors; this cyan color vanishes in presence of base (ammonia vapors). A reusable paper‐strip‐based method based on this self‐assembled fluorescent material can be used to easily detect hazardous volatile acid and base vapors with the naked eye. [ABSTRACT FROM AUTHOR]

Multiblock copolymers: A new method to synthesize functional multiblock copolymers composed of alternately aligned sequential peptides and vinyl polymers is described. Cyclic oligopeptides containing an alkoxyamine bond in the framework have been developed as an initiator for NMP. Radical polymerization by this type of initiator enables multiple peptide blocks to be directly inserted into the vinyl polymer backbone during the polymerization. Folding behavior of the resultant multiblock peptide–polymer hybrid is also demonstrated. For more information see the Full Paper by N. Higashi, T. Koga, et al. on page 15050 ff. [ABSTRACT FROM AUTHOR]

The cover picture presents the ultrastructural morphology of tetra‐phenylalanine assembly prepared by a solvent‐switching technique. Imaging was performed using high‐resolution scanning electron microscopy. Read more in the Full Paper by Gazit and co‐workers on page 756. [ABSTRACT FROM AUTHOR]

Overcoming resistance: Multidrug resistance (MDR) remains a major problem for effective chemotherapy. In this study, a smart stimulus ‐ responsive self ‐ assembled system (PD/VER nanogel), formed from a short peptide ‐ Dox prodrug (PD) and the P ‐ glycoprotein inhibitor Verapamil (VER), was successfully developed for overcoming MDR. Such inhibitor ‐ encapsulated nanogels could greatly enhance the accumulation of drugs in resistant cancer cells, thereby effectively reversing tumor resistance. More information can be found in the Full Paper by Fang Liu, Bengang Xing et   al. on page   744 in Issue 7, 2017 (DOI: 10.1002/asia.201601704). [ABSTRACT FROM AUTHOR]