Leishmaniasis is a neglected tropical disease caused by the Leishmania parasite, primarily seen in developing and underdeveloped countries. Due to immigration to our country, the effective population of the disease has increased recently. The lesion, which has visceral and cutaneous forms, can be lethal when it acts on internal organs. Surface proteins are the most crucial part of the parasite and host interaction. The parasite attaches to the host cell through surface proteins, enters the cell, multiplies, suppresses the immune system, and allows many other biological functions. It is the most critical research part in vaccine and biomarker discovery. Generally, cell surface biotinylation and cationic colloidal silica beads with which the surface is coated are used to analyze surface proteins. These methods break down the cell and are more open to contaminant proteins from the cytoplasm and nucleus. In addition, since the surface proteins are rich in hydrophobic amino acids, they are difficult to dissolve in polar solvents. The shaving method, uses a faster and minimal experimental workflow to cut only cell surface proteins without lysing the cell, has been tried in four Leishmania species (L.Tropica, L.Infantum, L.Major, L.Donovani). The shaving method aims to digest cell surface proteins by treating the cell surface with a proteolytic enzyme for a short time. Thus, it is expected to contain fewer contaminants and unwanted proteins. As a result of shaving method analysis with the Fusion Orbitrap Mass Spectrometer, the rate of surface protein defined in 4 different species was 9.34% in L.Tropica, 7.55% in L.Major, 7.9% in L.Infantum, 7.52% in L.Donovani. Consistent with the literature and candidates for biomarker ISCL, KMP-11, Leishmanolysin, PSA-2, ABC transporter, and lanosterol 14α demethylase, proteins were identified. Familiar and different proteins were tabulated.