Sickle hemoglobin aggregation: a new class of inhibitors

Abstract

A number of tri- and tetrapeptides have been found to inhibit aggregation and gelation of deoxygenated sickle cell hemoglobin. These inhibitors have hydrophobic phenylalanine residues at one end and hydrogen bonding lysine or arginine side chains at the other end. The backbone is not very specific. The inhibitors do not modify the oxygen carrying properties of hemoglobin. When the inhibitor and sickle hemoglobin are put inside reconstituted cells, the erythrocytes do not sickle upon deoxygenation. Compounds of this type may develop useful agents in the therapy of sickle cell anemia.