Myeloma (MM) is an incurable malignancy due to unsuccessful elimination of minimal residual disease (MRD). Current standard chemotherapeutic treatments that target apoptotic cell death pathways have proven to be unsuccessful in curing this disease, due to emergence of drug resistance. Recently Hazlehurst and co-workers have reported an all d-amino acid peptide HYD1 that induces necrotic cell death in MM. Several strategies aiming to enhance the potency of this linear d-amino acid peptide led to the discovery of a novel cyclic peptide we named MTI-101. MTI-101 and its analogs bind to the extracellular domain of CD44 and kills MM cells as a single agent via a necrosis pathway. According to surface plasmon resonance experiment MTI-101 binds to an ectodomain of CD44 with high affinity (KD ∼ 10 nm). To optimize the PK of MTI-101, we have identified a site for peforming bioconjugation of pegylating reagents and specific multimers of MTI analogs. Herein, we report several bioconjugation strategies that aim to increase the circulating half-life of peptide MTI-101 analogs for the treatment of MM.