During solid phase peptide synthesis, the side chains of the amino acids cysteine and selenocysteine must be protected due to the high nucleophilicity of the thiol and selenol groups. Two protecting groups that have been used for these amino acids are the p-methoxybenzyl (pMob) and acetamidomethyl (Acm) groups. Trifluoroacetic acid (TFA) is widely used to release peptides from the solid support and to remove side chain protecting groups in a one-step process. But the pMob and Acm protecting groups are acid stable, thus requiring harsher conditions for removal, conditions that lead to side reactions. Robert Hondal and co-workers have developed new deprotection chemistry for removing pMob and Acm from cysteine and selenocysteine. The method is mild and utilizes a commercially available reagent, the aromatic disulfide 2,2'-dithiobis(5-nitropyridine) (DTNP). A mixture of DTNP, TFA, and thioanisole removes the pMob and Acm groups from the thiol of cysteine. The pMob group of selenocysteine is removed using DTNP and TFA without thioanisole. There are many avenues to explore with this new deprotection chemistry, including: 1) Testing the chemistry out on other cysteine side chain protecting groups, focusing on commercially available derivatives (trityl, benzyl, paramethylbenzyl, t-butyl and S-t-butyl). 2) Using selenoanisole as a catalyst in place of thioanisole, believing that it will be more effective due to the greater nucleophilicity of selenium. 3) Exploring other aromatic disulfides in place of DTNP. This work is on-going and we are optimistic that the outcome will be better methods to remove protecting groups from cysteine and selenocysteine residues.