Alloc-Val-Ala-PAB-OH

Alloc-Val-Ala-PAB-OH is a cleavable ADC linker designed for precise antibody-drug conjugate (ADC) construction and targeted bioconjugation applications. Featuring an allyloxycarbonyl (Alloc) protecting group, a valine-alanine dipeptide (Val-Ala) sequence, and a p-aminobenzyl (PAB) self-immolative spacer, this linker enables site-specific attachment of ADC cytotoxins. The Val-Ala dipeptide provides protease-sensitive cleavability, allowing selective intracellular payload release in lysosomal compartments. In ADC linker design, Alloc-Val-Ala-PAB-OH maintains antibody integrity while offering modular conjugation options for enhanced solubility, stability, and therapeutic performance.

In payload conjugation applications, Alloc-Val-Ala-PAB-OH is compatible with a wide range of ADC cytotoxins, including microtubule inhibitors and DNA-targeting agents. The Alloc protecting group shields reactive functionalities during synthesis, while the PAB spacer enables rapid self-immolative release of payloads upon intracellular proteolytic cleavage. The Val-Ala sequence is selectively recognized by lysosomal proteases, ensuring precise and efficient payload release in tumor cells. Researchers can leverage this linker to construct homogeneous, stable ADCs with predictable pharmacokinetics and optimized therapeutic activity.

From an application perspective, Alloc-Val-Ala-PAB-OH is extensively used in oncology-focused ADC research, targeted drug delivery studies, and protease-sensitive bioconjugation strategies. Its combination of Alloc protection, Val-Ala protease-cleavable sequence, and PAB self-immolative spacer ensures efficient, site-specific conjugation while preserving antibody structure. Incorporating this linker into ADC designs enables the creation of stable, functional linker-payload conjugates that release cytotoxic agents selectively within tumor cells, enhancing therapeutic precision and effectiveness.