Proteins constitute the majority of nature's worker biomolecules. Designed for specific
functions, complex tertiary structures make proteins ideal candidates for analysing natural …

Peptides are a growing therapeutic class due to their unique spatial characteristics that can
target traditionally “undruggable” protein–protein interactions and surfaces. Despite their …

Proteins are the most abundant biomolecules within a cell and are involved in all
biochemical cellular processes, fulfilling specific functions with unmatched precision. This …

Site-selective chemical conjugation of synthetic molecules to proteins expands their
functional and therapeutic capacity. Current protein modification methods, based on …

Combining the selective targeting of tumor cells through antigen-directed recognition and
potent cell-killing by cytotoxic payloads, antibody-drug conjugates (ADCs) have emerged in …

Chemists, biologists, and material scientists alike have long sought to control protein
presentation, orientation, and activity within biomaterials to dictate reaction catalysis …

Site‐selective protein functionalization serves as an invaluable tool for investigating protein
structures and functions in complicated cellular environments and accomplishing semi …

Systematically dissecting the molecular basis of the cell surface as well as its related
biological activities is considered as one of the most cutting-edge fields in fundamental …

Diethynyl phosphinates were developed as bisfunctional electrophiles for the site‐selective
modification of peptides, proteins and antibodies. One of their electron‐deficient triple bonds …

Nature has evolved an optimal synthetic factory in the form of translational and
posttranslational processes by which millions of proteins with defined primary sequences …