The present invention provides peptoid polymers capable of reducing or inhibiting the formation of ice crystals at sub 0° C. temperatures. Also provided are peptoid-peptide hybrids comprising the peptoid polymers provided herein. The peptoid polymers and peptoid-peptide hybrids provided herein are useful for making cryoprotectant solutions. The peptoid polymers, peptoid-peptide hybrids, and cryoprotectant solutions provided herein are useful for making antifreeze solutions, frozen food products, and cosmetic care products. Also provided herein are methods for preserving a tissue, an organ, a cell, or a biological macromolecule using the compositions described herein.

The present disclosure provides novel polypeptide conjugates. The polypeptide conjugates disclosed herein comprise a stapled peptide comprising a peptide and at least one staple which holds the peptide in an α-helical conformation, and a cyclic cell-penetrating peptide (cCPP) conjugated, directly or indirectly, to the stapled peptide. The present disclosure demonstrates that cCPPs can be used to confer consistent cell-permeability to stapled peptides.

Disclosed herein are compositions and methods suitable for treating acute leukemia by inhibiting π π π stacking in the YEATS protein domain. YEATS protein domains are typically found in a variety of chromatin modification molecular complexes. Cancer cells are characterized by aberrant epigenetic landscapes and often exploit chromatin machinery to activate oncogenic gene expression programs. Quantitative analysis of the inhibitory activity of YEATS domain inhibitors by use of a fluorescence-based assay revealed that several of the tested inhibitors achieved 50% inhibition at the submicro/nanomolar level. As such, provided is the use of small molecule inhibitors that target the ENL YEATS domain to selectively kill leukemic MLL-r cells.

A polypeptide, a photoresist composition including the polypeptide, a photoresist including the polypeptide, and a method of forming patterns using the photoresist composition.

A lipid composition containing a nucleic acid, wherein the lipid composition comprises a peptide-lipid conjugate, is provided. The peptide of the peptide-lipid conjugates can be from 4 to 52 amino acids in length. Methods of using the lipid composition in the in vivo delivery of nucleic acids are further provided.

Provided herein are hierarchical protein structures comprising two or more proteins extending in one or more dimensions, the hierarchical protein structure comprising: a first protein comprising: (i) a patch A comprising one or more polynucleotides conjugated to the surface of the first protein; and (ii) a patch B comprising one or more polynucleotides conjugated to the surface of the first protein; and a second protein comprising: (i) a patch A′ comprising one or more polynucleotides conjugated to the surface of the second protein; and (ii) a patch B′ comprising one or more polynucleotides conjugated to the surface of the second protein; wherein the one or more polynucleotides of the patch A hybridizes to the one or more polynucleotides of the patch A′, and/or the one or more polynucleotides of the patch B hybridizes to the one or more polynucleotides of the patch B′ to form the hierarchical protein structure. Also provided are methods of making the hierarchical protein structures.

A peptoid compound, a manufacturing method of a peptoid compound, an oligomer, a pharmaceutical composition, use of the pharmaceutical composition in the preparation of a medicament for detecting or diagnosing a disease related to tyrosine kinase HER2, and a kit for identifying circulating tumor cells are provided, the peptoid compound includes: a cysteine (Cys) subunit, a butanediamine (Nlys) subunit, a 3,4-methylenedioxybenzylamine (Npip) subunit, a 3-aminopropanic acid (Nce) subunit and a 1-naphthylamine (Na) subunit, and both the peptoid compound and the oligomer have a strong ability to bind to HER2 protein on surfaces of circulating tumor cells (CTCs), and a technology of diagnosing breast cancer on the basis of the peptoid compound can realize non-invasive and label-free rapid diagnosis, in addition, the methods for synthesizing the peptoid compound and the oligomer are simple, the preparation efficiency is high, and the production cost is low.

The present application provides: a polypeptide characterized by having an ability of penetrating into a cell and the structure represented by Formula (I) ##STR00001##
wherein n is a number of 2 to 20; R.sup.1 and R.sup.2 may independently represent a C.sub.1-C.sub.4 alkyl group or may bind to each other to form a ring; R.sup.3 represents a C.sub.1-C.sub.10 primary aminoalkyl group; R.sup.4 represents a hydrogen atom or a C.sub.1-C.sub.10 hydrocarbon group; the “n” number of R.sup.1, R.sup.2, R.sup.3, and R.sup.4 may independently be the same with or different from each other; and the N-terminus and the C-terminus may or may not be modified independently; and a cell-invasive composition comprising the polypeptide and a substance of interest.

Methods and compositions are presented for use in diagnostic, imaging or targeting of therapeutic agents to treat cancer cells in metastases. such as where compositions and methods identify and employ peptides to selectively target cancer cells in metastases in mammals, both in vitro and in vivo.

An objective is to provide an Fc-modified antibody or the like having a long serum half-life according to a CCAP method, more specifically, an antibody or the like where IgBP is bound to only one site, based on findings of the inventors. Provided is an objective antibody or the like by purification and production of an Fc-modified antibody or the like with a column bound to an Fc region of an antibody. Specifically, an antibody where only one of two binding sites of Fc is selectively modified is provided by allowing an IgBP-bound antibody produced by a CCAP method to adsorb to a carrier of an IgBP-immobilized column, or forming a state where only one Fc of an antibody is bound to an IgBP binding column and then adding a peptide reagent for CCAP to the column to perform a reaction of a CCAP method in the column.